用户名: 密码: 验证码:
牛肉肌内结缔组织变化对其嫩度影响的研究
详细信息    本馆镜像全文|  推荐本文 |  |   获取CNKI官网全文
摘要
我国是牛肉生产大国,但牛肉嫩度较差,除了历史原因(牛作为一种使役工具)外,关键是对我国黄牛肉品质的系统研究较晚。影响牛肉嫩度的外在因素很多,但所有外在因素的作用都是通过影响内在因素(肌原纤维、肌内结缔组织和肌内脂肪)而实现的,且各因素对牛肉嫩度的作用机制不尽相同,学术界还存在较多争议。本研究结合我国牛肉生产的实际情况,针对目前尚存在争议的科学问题,从生理成熟度、大理石花纹、分割部位、宰后成熟、加热等对牛肉嫩度及其相关指标影响的研究,旨在重点揭示肌内结缔组织变化对牛肉嫩度的影响。
     本研究主要围绕我国牛肉分级标准(生理成熟度、大理石花纹和分割部位)和屠宰加工工艺(宰后成熟和加热)开展系列研究。内容共包括五个部分:一、加热温度对牛肉嫩度影响的研究;二、生理成熟度对牛肉嫩度影响的研究;三、大理石花纹对牛肉嫩度影响的研究;四、宰后成熟对牛肉嫩度影响的研究;五、牛背最长肌和半腱肌嫩度的比较研究。具体研究内容和结果如下:
     1.加热温度对牛肉嫩度影响的研究
     通过对牛肉加热过程中嫩度及相关食用品质指标的变化研究,阐述加热对嫩度影响的可能机制。选择宰后96h牛半腱肌,分别加热到40,50,55,60,65,70,75,80,85和90℃。随后进行化学测定、嫩度测定和组织学观察。结果表明,加热初期,水分含量和次级肌束膜厚度降低(P<0.05),而粗脂肪和结缔组织滤渣含量增加(P<0.05)。随着加热温度(65℃以上)进一步升高,水分含量进一步下降,而剪切力值增加(P<0.05)。整个加热过程中,结缔组织滤渣持续增加,而肌纤维直径持续降低(P<0.05)。剪切力值与水分含量、粗脂肪含量、结缔组织滤渣、肌纤维直径和肌束膜厚度显著相关(P<0.05)。热示差扫描分析表明肌内膜的最大变性温度比肌束膜低(50.2℃vs.65.2℃)。对于牛半腱肌来说,65℃是保证牛肉嫩度和品质的关键加热温度。肌纤维和肌束膜的性质和状态决定着牛肉的嫩度。两者所起作用的大小因加热温度的变化而改变,65℃以下时,肌纤维起主要作用,胶原蛋白也起一定的作用;75℃以上,胶原蛋白起主要作用。
     2.生理成熟度对牛肉嫩度影响的研究
     通过对牛肉嫩度及相关指标随牛胴体生理成熟度变化的研究,阐述牛肉嫩度随生理成熟度变化的相关机制。对胴体生理成熟度为A、C和E、成熟96h的牛半腱肌进行化学测定、组织学观察和机械测定。结果表明,蒸煮损失、熟肉剪切力值、粗脂肪含量及肌纤维直径随生理成熟度的增加而增加(P<0.05)。同一肉块内不同部位间、同一生理成熟度组内不同肉块之间各指标测定值之间存在很大差异。剪切力值与原料肉中水分含量和肌节长度、蒸煮损失、熟肉中总胶原蛋白含量、肌节长度和肌纤维直径显著相关(P<0.05)。胴体生理成熟度对牛肉嫩度的影响具有阶段性,体成熟前,结缔组织特性的变化是导致嫩度下降的主要因素;体成熟后肌纤维特性和肌内脂肪含量的变化是引起嫩度变化的主要因素。
     3.大理石花纹对牛肉嫩度影响的研究
     比较研究了不同大理石花纹等级的牛肉嫩度及相关指标,并据此说明了牛肉嫩度变化的相关机制。对大理石花纹等级为少量(3)、丰富(2)和极丰富(1)、成熟96h的牛背最长肌进行化学测定、组织学观察和机械测定。结果表明,粗脂肪含量、胶原蛋白含量、肌纤维直径及肌内结缔组织的最大热变性温度随大理石花纹的增加而增加(P<0.05);蒸煮损失、胶原蛋白可溶性、剪切力值、肌束膜厚度随大理石花纹的增加而下降(P<0.05)。同一肉块内不同部位间、同一大理石花纹组内不同肉块之间各指标测定值之间存在很大差异。剪切力值与水分含量、粗脂肪含量、胶原蛋白含量、肌节长度、蒸煮损失及肌束膜厚度显著相关(P<0.05)。大理石花纹的沉积过程中使肌束膜内部胶原纤维排列发生改变、避免了宰后冷却过程中肌纤维收缩、降低了加热过程中蒸煮损失,从而使牛肉嫩度得到提高。
     4.宰后成熟对牛肉嫩度影响的研究
     跟踪研究了牛肉嫩度及相关指标宰后成熟过程中的变化,并据此阐明宰后成熟中结缔组织变化对牛肉嫩度的影响。选择宰后96h牛半腱肌,0-4℃条件下继续成熟7、10、17、24d。随后进行化学测定、嫩度测定和组织学观察。结果表明,成熟过程中,水分含量、胶原蛋白可溶性和蒸煮损失增加(P<0.05),而结缔组织滤渣含量、初级肌束膜厚度、肌纤维直径、肌内膜热变温度、剪切力值下降(P<0.05)。剪切力值与熟肉的结缔组织滤和肌纤维直径显著相关(P<0.05)。在一个完整的宰后成熟期(约30d)内,牛肉嫩度得到改善,中后期(11d以后)主要是肌内结缔组织结构弱化作用所致。
     5.牛背最长肌和半腱肌嫩度的比较研究
     比较研究了牛背最长肌和半腱肌在宰后成熟中嫩度和相关指标的变化。选择宰后4d牛背最长肌和半腱肌,一半直接用于相关指标测定,另一半在0-4℃条件下继续成熟17d,随后进行化学测定、嫩度测定和组织学观察。结果表明,宰后第4d,背最长肌的水分含量和剪切力值高于半腱肌(P<0.05),而胶原蛋白和结缔组织滤渣低于半腱肌(P<0.05),宰后第21d,背最长肌水分含量、胶原蛋白含量、肌纤维直径比半腱肌小(P<0.05),而肌束膜厚度和胶原蛋白可溶性高于半腱肌(P<0.05)。成熟过程中,背最长肌肌内结缔组织结构更易遭到破坏。肌纤维和肌内结缔组织结构和性质的差异都是导致背最长肌和半腱肌嫩度差异的重要原因。宰后成熟可更有效的改善背最长肌的嫩度。
China is one of the biggest nations in beef production, but beef tenderness is poor. This is mainly attributed to, except for labor-force purpose, the lack of a systematic research on beef tenderness. Beef tenderness is influenced by the internal factors (myofibrillar components, intramuscular connective tissue, and intramuscular fat), which is, in turn, affected by many external factors by different ways. Meanwhile, there are still controversies on how to affect beef tenderness for a specific factor. Therefore, this study was designed to track the changes of beef tenderness and related characteristics with heating, carcass maturity, marbling, postmortem aging and anatomy, where more emphasis were placed upon the effects of IMCT on beef tenderness, and then to give some explanations for practical problems in beef production in China and also for some scientical problems.The paper includes the following five parts:Part I Effect of heating temperature on beef tendernessThe experiment was designed to explore the effect of heating on meat quality characteristics and IMCT of beef semitendinosus muscle, and then an explanation was given for how beef tenderness changed during heating. The semitendinosus steaks were cooked to 40, 50, 55, 60, 65, 70, 75, 80, 85, and 90℃respectively, and then were used for chemical determinations, mechanical and histological measurements. The results indicated that at the beginning of cooking, moisture and the secondary perimysial thickness decreased (P<0.05), whilst crude fat and filtering residues increased (P<0.05). Moisture content continued to decrease whilst WBSF increased (P<0.05) over 65℃. Through cooking, filtering residues increased continuously (P<0.05), concomitant with a gradual decline (P<0.05) for the fiber diameter. WBSF correlated (P<0.05) with percentages of moisture, crude fat, filtering residues, fiber diameter and perimysial thickness. The maximum transition temperature of endomysial components was lower than that of perimysial components (50.2℃vs. 65.2℃). 65℃is a critical cooking point to meat quality for beef semitendinosus muscle. WBSF is influenced by the natures of both myofibrillar components and intramuscular connective tissue. Below 65℃, the nature of myofibrillar components is the main contributor to beef tenderness, whilst that of intramuscular connective tissue is above 75℃.
     PartⅡEffect of carcass maturity on beef tenderness
     The experiment was designed to explore the effects of carcass maturity on meat quality characteristics and IMCT of beef semitendinosus muscle, and then an explanation was given for the mechanism of tenderness with maturity. Chemical determinations, histological and mechanical measurements were performed on the raw and cooked meat with maturities A, C and E at days postmortem. The results indicated that WBSF, cooking losses, crude fat content and fiber diameter of cooked meat increased (P<0.05) with the increase of carcass maturity. Great variations existed (P<0.05) for most of the measurements among cores within the same steak, and among individual steaks within the same maturity group. WBSF was correlated significantly (P<0.05) with moisture content, sarcomere length of raw meat, and cooking losses, total collagen content, sarcomere length and fiber diameter of cooked meat. Carcass maturity has a phase-in influence on beef tenderness, which is affected mainly by the traits of IMCT before body maturation, and then by the muscle fiber trait and IMF content.
     PartⅢEffects of marbling on beef tenderness
     The experiment was designed to explore the effects of marbling on meat quality characteristics and IMCT of beef longissimus muscle. Chemical determinations, histological and mechanical measurements were performed on the raw and cooked meat at 4 days postmortem. The results showed that crude fat, collagen, fiber diameter and maximum transition temperature of IMCT increased (P<0.05) with the increase of marbling score. The cooking losses, collagen solubility, WBSF and secondary perimysial thickness decreased (P<0.05) with the increasing marbling. WBSF correlated (P<0.05) with moisture, crude fat, collagen, cooking losses, sarcomere length and secondary perimysial thickness. The development of marbling results in the disorganization of the perimysia, the avoidance of sarcomere shortening during chilling, and the decline in cooking losses, which accounts for the improvement of beef tenderness.
     PartⅣEffect of postmortem aging on beef tenderness
     This part was designed to find out the effect of postmortem aging on meat quality characteristics and IMCT of beef semitendinosus muscle. ST muscles were obtained at 4 days postmortem. Chemical determinations, histological and mechanical measurements were performed for the raw and cooked steaks at 4, 11, 14, 21, and 28 days postmortem, respectively. The results showed that postmortem aging resulted in an increase in percent moisture, collagen solubility, and cooking losses, and a decrease in filtering residues, primary perimysial thickness, fiber diameter, WBSF, and transition temperature of the endomysium. WBSF correlated with the quantity of filtering residues and the fiber diameter of cooked meat. Beef tenderness is improved within a whole period of postmortem aging (about 30 days), which is mainly attributed to the weakening of intramuscular connective tissue over 11 days.
     PartⅤA comparison of tenderness between beef longissimus and semitendinosus
     This part was designed to compare meat quality characteristics and the traits of IMCT of beef longissimus (LM) and semitendinosus (ST) muscles at 4 and 21 days postmortem. Meat samples were obtained at 4 days and one halves were aged till 21 days. Chemical determinations, histological and mechanical measurements were performed on the raw and/or cooked meat. The results showed that LM had higher (P<0.05) moisture content and WBSF, but lower (P<0.05) collagen content and filtering residues than ST at 4 days. At 21 days, LM had lower (P<0.05) moisture content, collagen content and fiber diameter, but higher (P<0.05) perimysial thickness and collagen solubility than ST. The structure of LM IMCT was more liable to aging-induced destruction than ST. Both the nature of muscle fiber and the traits were the contributors to the differences in tenderness between the two muscles. Aging is more efficient to improve tenderness of LM than for ST.
引文
[1] 中华人民共和国统计局.中国统计年鉴1990[M] .中国统计出版社,北京,1990
    [2] 中华人民共和国统计局.中国统计年鉴1997[M].中国统计出版社,北京,1997
    [3] 中华人民共和国统计局.中国统计年鉴2001[M].中国统计出版社,北京,2001
    [4] 中华人民共和国统计局.中国统计年鉴2003[M].中国统计出版社,北京,2003
    [5] 中华人民共和国统计局.中国统计年鉴2005[M] .中国统计出版社,北京,2005
    [6] 李静.世界三大产肉国主要肉类生产情况对比[J].饲料广角,2005,6:35-37
    [7] 高腾云,张云涛,宋洛文.我国肉牛业的现状及市场分析[J].养殖技术顾问,2005,9:43
    [8] 约翰 W 朗沃斯等编.刘玉满译.中国肉牛业的商务机遇与挑战[M] .中国农业出版社,北京,2003.
    [9] 周光宏主编.肉品学[M] .中国农业科技出版社,北京,1999
    [10] 吕礼良等.国内外肉牛生产现状及发展对策[J].延边大学农学学报,2004,26(4):308-312
    [11] 刘丽,周光宏.我国优质牛肉生产概况[J].黄牛杂志,1998,24(4):32-34
    [12] USDA. United States standards for grades of carcass beef. Agriculture Marketing Service, USDA, Washington, DC, 1997.
    [13] Agriculture and Agri-food Canada. Live Cattle Ultrasound and the Canadian Beef Grading System. Available: www.agr.gov.sk.ca/DOCS/livestock/beef/marketing/ultrasound.asp.Assessed:Jan 20,2006.
    [14] 高档牛肉标准.Avail:http://www.agric138.com.cn/subhome/xm/tech/cattle/syjs_rn/gdbj.htm. Accessed: Jan, 10, 2006.
    [15] AUS-MEAT. Handbook of Australian meat (6th edition) [M]. Australian Meat and Livestock Corporation, Brisbane, Queensland, Australia, 1998.
    [16] Meat Livestock Australia. Meat Standards Australia [M]. Australia, 2003
    [17] 日本食肉规格付协会.平成13年.牛·豚·枝肉·部分肉取引规格解说书.
    [18] 赵玉民,张云影等.日本肉牛业的特点及其发展战略.延边大学农学学报,1997,19(2):128-131
    [19] Kyung C K. Chapter 15. Meat marketing and grading system in Korea. Available: agis.nlri.go.kr/korea/library/Book/upload/P1/B04-14.PDE Accessed: Jan 10, 2006
    [20] Park G B, Moon S S, et al. Influence of slaughter weight and sex on yield and quality grades of Hanwoo (Korean native cattle) carcasses [J]. Journal of Animal Science, 2002, 80: 129-136.
    [21] 中国农业部.牛肉质量分级[M] .中国标准出版社,北京,2003
    [22] 孙宝忠,马爱进等.牛肉质量评定分级标准现状、制定原则及作用[J].中国食物与营养,2002(5):15-16
    [23] 刘成国,骆承庠,刘希良.不同电刺激条件对牛肉嫩度的影响[J].肉类研究 1993(3):12-15
    [24] 刘成国,骆承庠,刘希良.电刺激与热剔骨对牛肉嫩度的影响[J].肉类研究,1992(1):6-9
    [25] 祝贵希,王方来等.优质高档牛肉生产技术研究报告[J].黄牛杂志,1995,21(1):14-17
    [26] 蒋洪茂.我国黄牛肉用性能研究报告(上)[J].黄牛杂志,1996,22(3):3-10
    [27] 蒋洪茂.我国黄牛肉用性能研究报告(下)[J].黄牛杂志,1996,22(4):28-31
    [28] 吴克谦,陈雪秀等.肉牛肥育与高档牛肉分割测定试验[J].黄牛杂志,1997,23(3):14-19
    [29] 刘丽,周光宏.预测黄牛及其改良牛牛肉嫩度的胴体形状筛选[J].南京农业大学学报,2001, 24{2):106-109
    [30] 刘丽,周光宏.饲养水平、年龄及体重对牛产肉性能影响的研究[J] .黄牛杂志,2001,27(3):9-14
    [31] 王丽哲,刘丽,周光宏.品种、年龄及活重对产肉性能的影响[J] .黄牛杂志,2001,27(4):12—16
    [32] 黄明,周光宏等.未育肥黄牛的产肉性能与牛肉食用品质的研究[J] .食品科学,2002,23(9):33-36
    [33] 陈银基,周光宏等.中国黄牛及其杂交牛产肉量和产肉率预测[J] .安徽农业科学,2005,33(7):1234-1237
    [34] 刘丽,王丽哲,周光宏.应用模糊数学评定牛肉的品质[J].肉类工业,2001(8):27-29
    [35] 黄明,周光宏等.不同日粮水平和成熟时间对牛肉质量的影响[J] .南京农业大学学报,2003,26(2):93-96
    [36] 汤晓艳,周光宏,徐幸莲.不同质量等级的中国黄牛肉在成熟过程中的品质变化研究[J] .食品科学,2005,26(4):66-69
    [37] 罗欣,黄明,朱燕.电刺激技术在牛肉快速成熟中的应用研究[J] .农业工程学报,2001,17(6):127-131
    [38] Li et al. Effects of low-voltage electrical stimulation and pre-rigor rapid chilling on meat quality characteristics for Chinese crossbred bulls [J]. Meat Science, 2006,
    [39] 靳烨,南庆贤.牛肉高压嫩化工艺参数的研究[J] .食品与机械,2001(4):23-25
    [40] 靳烨,南庆贤,车荣钲.高压处理对鲜牛肉感官性能的影响[J] .肉类研究,1998(4):19-21
    [41] 靳烨,南庆贤.高压处理对牛肉感官特性与食用品质的影响[J] .农业工程学报,2004,20(5):196-199
    [42] 马汉军,周光宏等 高压处理对牛肉肌红蛋白及颜色变化的影响[J] .食品科学,2004,25(12):36-39
    [43] 马美湖,唐晓峰.氯化钙和木瓜蛋白酶对牛肉嫩化效果的研究[J] .湖南农业大学学报(自然科学版),2001,27(1):63-66
    [44] 马美湖,唐晓峰.可溶性胶原蛋白含量、MFI、CAF与牛肉嫩化的关系[J] .肉类研究,2001(2):16-20
    [45] 韩玲.冷却牦牛分割肉酶嫩化技术研究[J] .农业工程学报,2003,19(2):171-175
    [46] 赵立艳,彭增起,陈贵堂.磷酸盐对牛肉嫩化作用的研究[J] .食品工业科技,2003,24(5):27-28
    [47] 黄明,罗欣.热处理对牛肉剪切力值及蒸煮损失的影响[J] .肉类工业,1999(10):24-26
    [48] 曾勇庆,孙玉民.鲁西黄牛与利鲁杂交牛肉质特性的研究[J] .黄牛杂志,1999,25(3):12-16
    [49] 李福吕,李同树等.渤海黑牛肉品品质的研究[J] .黄牛杂志,2001,27(1):12-15
    [50] 喻兵兵,毛华明,文际坤.优质肉牛屠宰试验及肉品质研究[J] .云南农业大学学报,2004,19(2):215-219
    [51] 范江平,叶绍辉等,杂交大额牛肉质特性研究初报[J] .云南农业大学学报,2005,20(4):600-602
    [52] 王奎明,张春艳.宰后成熟对牛肉品质的影响[J] .肉类工业,2001(4):21-24
    [53] 汤晓艳,周光宏等.钙离子溶液浸泡处理对牛肉肌原纤维的影响[J].南京农业大学学报,2004,27(3):95-98
    [54] 赵改名,田玮等.钙离子活化酶系统与牛肉嫩度的关系[J] .河南畜牧兽医,2000,21(2):7-9
    [55] 黄明,周光宏等.牛肉宰后嫩化机制研究[J] .农业工程学报,2004,20(1):198-202
    [56] 黄明,赵莲等.钙离子和钙激活酶外源抑制剂对牛肉钙激活酶活性和超微结构的影响[J] .南京农业大学学报,2004,27(4):101-104
    [57] Torrescano G., Sanchez E. A., Gimenez B., et al. Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics [J]. Meat Science, 2003, 64: 85-91.
    [58] Herring H K, Cassens R G, Suess G G, et al. Tenderness and associated characteristics of stretched and contracted bovine muscle [J]. Journal of Food Science, 1967, 32: 317-323
    [59] Wheeler T L, Koohmaraie M. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major [J]. Journal of Animal Science, 1999, 77: 2444-2451
    [60] Taylor R G. Meat tenderness: theory and practice [M]. Proceedings of 49th International Congress of Meat Science and Technology, 2003: 56-66.
    [61] Kooharaie M, Shalkelford S D, Wheeler T L, et al. A muscle hypertrophy condition in lamb (callipyge): characterization of the effects on muscle growth and meat quality traits [J]. Journal of Animal Science, 1995, 73: 3596-3607.
    [62] Kooharaie M, Shalkelford S D, Wheeler T L. Effects of a β-adrenergic agonist (L644, 969) and male sex condition on muscle growth and meat quality of callipyge lamb [J]. Journal of Animal Science, 1996, 74: 70-79.
    [63] Locker R H Cold induced toughness of meat. In: Advances in meat research vol I-electrical stimulation [M]. Eds. A M Pearsonn, T R Duston. AVI Publishing Co. Inc, Westport, C T, pp, 1-44, 1985
    [64] Crouse J D, Koohmaraie M, Seideman S D. The relationship of muscle fibre size to tenderness of beef [J]. Meat Science. 1991, 30; 295-302
    [65] Lewis P K, Brown C J, Heck M C. Fiber diameter, sarcomere length and tenderness of certain muscles of crossbred beef steers [J]. Journal of Animal Science, 1977, 45: 254-260
    [66] Tuma H J, Venable J H, Wuthier P R, et al. Relationship of fiber diameter to tenderness and meatiness as influenced by bovine age [J]. Journal of Animal Science, 1962, 21:33-36
    [67] DeSmer S, Claeys E, Buysse G, et al. Tenderness measurement in four muscles of Belgian Blue normal and double muscled bulls [M]. Proc 44th ICoMST, pp, 288-289
    [68] Romans J R, Tuma H J, Tucker W L. Influence of carcass maturity and marbling on the physical and chemical characteristics of beef, palatability, fiber diameter and proximate analysis [J]. Journal of Animal Science, 1966, 25: 681-685
    [69] Lawrance T E, Whatley J D, Montgomery T H, et al. Influence of dental carcass maturity classification on carcass traits and tenderness of longissimus steaks from commercially fed cattle [J]. Journal of Animal Science, 2001, 79: 2092-2096
    [70] Olson D G, Parrish F C, Stromer M H. Myofibril fragmentation and shear force resistance of 3 bovine muscles during postmortem storage [J]. Journal of Food Science, 1976, 41: 1036-1041
    [71] Takahashi K, Fukazawa T, Yasui T. Formation of myofibrillar fragments and reversible contraction of sarcomeres in chicken pectoral muscle [J]. Journal of Food Science, 1967, 32: 409-413
    [72] Kolczak T, Pospiech E, Palka K, et al. Changes of myofibrillar and centrifugal drip proteins and shear force of psoas major and minor and semitendinosus muscles from calves, heifers and cows during post-mortem ageing [J]. Meat Science, 2003, 64: 69-75
    [73] Kolczak T, Pospiech E, Palka K, et al. Changes in structure of psoas major and minor and semitendinosus muscles from calves, heifers and cows during post-mortem ageing [J]. Meat Science, 2003, 64: 77-83.
    [74] Olson D G, Parrish F C, Dayton W R, et al. Effect of postmortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle [J]. Journal of Food Science, 1977, 42: 117-124.
    [75] Koohmaraie M. The role of endogenous proteases in meat tenderness [J]. Reciprocal Meat Conference Proceedings, 1988, 41: 89-100
    [76] Koohmaraie M. Role of the neutral proteinases in postmortem muscle protein degradation and meat tenderness [J]. Reciprocal Meat Conference Proceedings, 1992, 45: 63-74
    [77] 黄明.牛肉成熟机制及食用品质研究[D] .南京农业大学博士论文,2003
    [78] Takahashi K. Mechanism of meat tenderization during postmortem ageing: calcium theory [J]. ICoMST 45th Proceedings. 1999, pp 230-235.
    [79] Lamare M, Taylor R G., Farout L, et al. Changes in proteasome activity during postmortem aging of bovine muscle [J]. Meat Science, 2002, 61: 199-204
    [80] Goll D E. Role of proteinases and protein turnover in muscle growth and meat quality [J]. Reciprocal Meat Conference Proceedings, 1991, 44: 25-36.
    [81] 张光玉,许梓荣.胶原蛋白交联的研究进展及其对肉的纹理和嫩度的影响[J] .国外畜牧科技,2001,28(2):41-46
    [82] Baily A J. Connective tissue and meat quality[J]. Reciprocal Meat Conference Proceedings, 1990, 43: 152-160
    [83] 陶凯忠,陈尔瑜,丁光宏.胶原纤维的结构和生物力学[J] .解剖科学进展,1998,4(4):289-293
    [84] 刘世新.实用生物组织学技术[M] .科学出版社,北京,2004
    [85] 孙丰梅,刘安军.胶原蛋白与肉品品质[J] .食品工业科技,2002(4):76-78
    [86] Shorthose W R, Harris P V. Effect of animal age on the tenderness of selected beef muscles [J]. Journal of Food Science, 1990, 55: 1-8
    [87] Young O A, Braggins T J. Tenderness of ovine semimembranosus: is collagen concentration or solubility the critical factor [J]. Meat Science, 1993, 35: 213-222
    [88] Fang S H, Nishimura T, Takahashi K. Relationship between development of intramuscular connective tissue and toughness of pork during growth of pigs [J]. Journal of Animal Science, 1999, 77: 120-130
    [89] McCormick R J. The flexibility of the collagen compartment of muscle [J]. Meat Science, 1994, 36: 79-85
    [90] Bosselmann A, Moller C, Steinhart H, et al. Pyridinoline crosslinks in bovine muscle collagen [J]. Journal of Food Science, 1995, 60: 953-958
    [91] Judge M D, Aberle E D. Effect of chronological and postmortem aging on thermal shrinkage temperature of bovine intramuscular collagen [J]. Journal of Animal Science, 1982, 54: 68-71
    [92] King N L. Thermal transition of collagen in ovine connective tissues [J]. Meat Science, 1987, 20: 25-37
    [93] Cross H R, Carpenter Z L, Smith G C. Effects of intramuscular collagen and elastin on bovine muscle tenderness [J]. Journal of Food Science, 1973, 38: 998-1003
    [94] Wheeler T L, Shackelford S D, Koohmaraie M. Technical notes: Sampling methodology for relating sarcomere length, collagen concentration, and the extent of postmortem proteolysis to beef and pork longissimus tenderness [J]. Journal of Animal Science, 2002, 80: 982-987
    [95] Miller R K, Tatum J D, Cross H R, et al. Effects of carcass maturity on collagen solubility and palatability of beef from grain-finished steers [J]. Journal of Food Science, 1983, 48: 484-486, 525
    [96] Avery N C, Sims T J, Warkup C, et al. Collagen crosslinking in porcine M. longissimus lumborum: absence of relationship with variation in texture at pork weight [J]. Meat Science, 1996, 42: 355-369
    [97] Burson D E, Hunt M C. Proportion of collagen type I and III in four bovine muscles differing in tenderness [J]. Journal of Food Science, 1986, 51: 51-53
    
    [98] Jeremiah L E, Dugan M E R, Aalhus J L, et al. Assessment of the relationship between chemical components and palatability of major beef muscles and muscle groups [J]. Meat Science, 2003, 65: 1013-1019
    [99] Casey J C, Crosland A R, Patterson R L S. Collagen content of Meat Carcasses of known history [J]. Meat Science, 1985, 12: 189-203
    
    [100] Nakamura Y N, Iwamoto H, Ono Y, et al. Relationship among collagen amount, distribution and architecture in the M. longissimus thoracis and M. pectoralis profundus from pigs [J]. Meat Science, 2003, 64: 43-50
    [101] Light N, Champion A E, Voyle C, et al. The role of epimysial, perimysial and endomysial collagen in determining texture in six bovine muscles [J]. Meat Science, 1985,13: 137-149.
    
    [102] McCormick R J. The influence of nutrition on collagen metabolism and stability [J]. Reciprocal Meat Conference Proceedings, 1989,42: 137-148
    
    [103] Sylvestre M N, Balcerzak D, Feidt C, et al. Elevated rate of collagen solubilization and postmortem degradation in muscles of lambs with high growth rates: possible relationship with activity of matrix metalloproteinases [J]. Journal of Animal Science, 2002, 80: 1871-1878
    [104] Crouse J D, Calkins C R, Seideman S C. The effects of rate of change in body weight on tissue development and meat quality of youth bulls. Journal of Animal Science, 1986, 63: 1824-1829
    [105] Listrat A, Rakadjiyski N, Jurie C, et al. Effect of the type of diet on muscle characteristics and meat palatability of growing Salers bulls [J]. Meat Science, 1999, 53: 115-124
    
    [106] Maiorano G, Manchisi A, Salvatori G, et al. Influence of multiple injections of vitamin E on intramuscular collagen and bone characteristics in suckling lambs [J]. Journal of Animal Science, 1999, 77: 2452-2457
    
    [107] Nold R A, Romans J R, Costello W J, et al. Characterization of muscles from boars, barrows, and gilts slaughtered at 100 or 110 kilograms: differences in fat, moisture, color, waterholding capacity, and collagen [J]. Journal of Animal Science, 1999, 77: 1746-1754
    
    [108] Nold R A, Unruh J A, Hunt M C, et al. Effects of implanting ram and wether lambs with zeranol at birth and weaning on palatability and muscle collagen characteristics [J]. Journal of Animal Science, 1992,70: 2752-2757
    [109] Burson D E, Hunt M C, Unruh J A, et al. Proportion of types I and III collagen in longissimus collagen from bulls and steers [J]. Journal of Food Science, 1986, 63: 453-456
    
    [110] Liu A, Nishimura T, Takahashi K. Relationship between structural properties of intramuscular connective tissue and toughness of various chicken skeletal muscles [J]. Meat Science, 1996, 43: 43-49
    
    [111] Brooks J C, Savell J W. Perimysium thickness as an indicator of beef tenderness [J]. Meat Science, 2004, 67: 329-344
    [112] Nishimura T., Hattori A., Takahashi K. Structural weakening of intramuscular connective tissue during conditioning of beef [J]. Meat Science, 1995, 39: 127-133
    [113] Nishimura T., Hattori A., Takahashi K. Relationship between degradation of proteglycans and weakening of the intramuscular connective tissue during postmortem ageing of beef [J]. Meat Science, 1996, 42: 251-260
    [114] Stanton C, Light N. The effects of conditioning on meat collagen: part 2-direct biochemical evidence for proteolytic damage in insoluble perimysial collagen after conditioning [J]. Meat Science, 1988, 23: 179-199
    [115] Stanton C, Light N. The effects of conditioning on meat collagen: part 3-evidence for proteolytic damage to insoluble perimysial collagen after conditioning [J]. Meat Science, 1990, 27: 41-54
    [116] Nishimura T, Liu A, Hattori A, et al. Changes in mechanical strength of intramuscular connective tissue during postmortem ageing of beef [J]. Journal of Animal Science, 1998, 76: 528-532
    
    [117] 王奎明,张春艳.宰后成熟对牛肉品质的影响[J].肉类工业,2001(4):21—24
    [118] Judge M D, Aberle E D. Effect of chronological and postmortem aging on thermal shrinkagetemperature of bovine intramuscular collagen [J]. Journal of Animal Science, 1982, 54: 68-71
    [119] Jeremiah L E, Dugan M E R, Aalhus J L, et al. Assessment of the relationship between chemical components and palatability of major beef muscles and muscle groups [J]. Meat Science, 2003, 65:1013-1019
    [120] Tuma H J, Henrickson R L, Stephens D F, et al. Influence of marbling and animal age on factors associated with beef quality [J]. Journal of Animal Science, 1962,21: 848-851
    [121] Wheeler T L, Cundiff L V, Koch R M. Effect of marbling degree on beef palatability in bos Taurus and bos indicus cattle [J]. Journal of Animal Science, 1994,72:3145-3151
    [122] Kerth C R, Montgomery J L, Lansdell J L, et al. Shear gradient in longissimus steaks [J]. Journal of Animal Science, 2002, 80: 2390-2395
    [123] Lawrance T E, Whatley J D, Montgomery T H, et al. Influence of dental carcass maturity classification on carcass traits and tenderness of longissimus steaks from commercially fed cattle [J]. Journal of Animal Science, 2001, 79: 2092-2096
    [124] Nishimura T, Hattori A., Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese black cattle: effect of marbling on beef tenderness [J]. Journal of Animal Science, 1999,77: 93-104
    [125] Brooks J C, Belew J B, Griffin D B, et al. National beef tenderness survey - 1998 [J]. Journal of Animal Science, 2000, 78:1852-1860.
    [126] Hiner R L, Hankins O G The tenderness of the beef in relation to different muscles and age in the animal [J]. Journal Animal Science, 1950,9: 347-353
    [127] Dunsing M. Visual and eating preferences of consumer household panel for beef from animals of different age [J]. Food Research, 1959, 12: 332-336
    [128] Simone M, Carroll F, Chickester C O. Differences in eating quality factors of beef from 18 and 30 month steers [J]. Food Technology, 1959,13: 337-341
    [129] Hiner R L, Hankins O G, Sloane H S, et al. Fiber diameter in relation to tenderness of beef muscle [J]. Food Research, 1953, 18: 364-376
    [130] Cornforth D P, Hecker A L, Cramer D A, et al. Maturity and its relationship to muscle characteristics of cattle [J]. Journal of Animal Science, 1980,50:75-80
    [131] Cross H R, Crouse J D, MacNeil M D. Influence of breed, sex, age and electrical stimulation on carcass and palatability traits of three bovine muscles [J]. Journal of Animal Science. 1984, 58: 1358-1365
    [132] Berry B W, Smith G C, Carpenter Z L. Beef carcass maturity indictors and palatability attributes [J]. Journal of Animal Science, 1974, 38: 507-514
    [133] Wythes J R, Shorthose W R. Chronological age and dentition effects on carcass and meat quality of cattle in northern Australia [J]. Australian Journal of Experimental Agriculture, 1991, 31: 145-152
    [134] Wulf D M, Page J K. Using measurements of muscle color, pH, and electrical impedance to augment the current USDA beef quality grading standards and improve the accuracy and prediction of sorting carcasses into palatability groups [J]. Journal of Animal Science, 2000, 78: 2595-2607
    [135] Kerth C R, Blair-Kerth L K, Jones W R. Warner-Bratzler shear force repeatability in beef longissimus steaks cooked with a convection oven, broiler, or clam-shell grill [J]. Journal of Food Science, 2003, 68: 668-670
    [136] Powell T. H., Dikemen M. E., Hunt M. C. Tenderness and collagen composition of beef semiteninousus roasts cooked by conventional convective cooking and modeled, multi-stage, convective cooking [J]. Meat Science, 2000, 55: 421-425
    [137] Hearne L E, Penfield M P, Goertz G E. Heating effects on bovine semitendinosus: shear, muscle fiber measurements and cooking losses [J]. Journal of Food Science, 1978, 43: 10-12,21
    [138] Hearne L E, Penfield M P, Goertz G E. Heating effects on bovine semitendinosus: phase contrast microscopy and scanning electron microscopy [J]. Journal of Food Science, 1978, 43: 13-16
    [139] Williams J R, Harrison D L. Relationship of hydroxyproline solubilized to tenderness of bovine muscle [J] . Journal of Food Science, 1978, 43: 464-467, 492
    [140] Wheeler T L, Koohmaraie M, Cundiff L V, et al. Effects of cooking and shearing methodology on variation in Warner-Bratzler shear force values in beef [J]. Journal of Animal Science, 1994, 72: 2325-2330
    [141] Wheeler T L, Shackelford S D, Koohmaraie M. Sampling, cooking, and coring effects on Warner-Bratzler shear force values in beef [J]. Journal of Animal Science, 1996, 74: 1553-1562
    [142] Powell T H, Hunt M C, Dikeman M E. Enzymatic assay to determine collagen thermal denaturation and solubilization [J]. Meat Science, 2000, 54: 307-311
    [143] Burson D E, Hunt M C. Heat induced changes in proportion of type 1 and III collagen in bovine longissimus dorsi [J]. Meat Science, 1986, 17: 153-160
    [144] Wu F Y, Dutson T R, Smith S B. A scanning electron microscopic study of heating-induced alterations in bovine connective tissue [J]. Journal of Food Science, 1985,50:1041-1044
    [145] Combes S, Lepetit J, Darche B, et al. Effect of cooking temperature and cooking time on Warner-Bratzler tenderness measurement and collagen content in rabbit meat [J]. Meat Science, 2003,66:91-96
    [146] Bouton P E, Harris P V, Ratcliff D. Effect of cooking temperature and time on the shear properties of meat [J] . Journal of Food Science, 1981, 46: 1082-1087
    [147] Christensen M, Purslow P P, Larsen L M. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibers and perimysial connective tissue [J]. Meat Science, 2000, 55: 301-307
    [148] Champion A E, Purslow P P, Duance V C. Dimensional changes of isolated endomysia on heating [J]. Meat Science, 1988, 24: 261-273
    [149] Palka K. Changes in intramuscular connective tissue and collagen solubility of bovine m. semitendinosus during retorting [J]. Meat Science, 1999,53: 189-194
    [150] Davey C L, Gilbert K V. Temperature-dependent cooking toughness in beef [J]. Journal of the Science of Food and Agriculture, 1974, 25: 931-938
    [151] Onenc A, Kaya A. The effects of electrical stunning and percussive captive bolt stunning on meat quality of cattle processed by Turkish slaughter procedures [J]. Meat Science, 2004, 66: 809-815
    [152] Denoyelle C, Lebihan E. Intramuscular variation in beef tenderness [J]. Meat Science, 2003, 66: 241-247
    [153] Kerth C R, Montgomery J L, Lansdell J L, et al. Shear gradient in longissimus steaks [J]. Journal of Animal Science, 2002, 80: 2390-2395
    [154] Reuter B J, Wulf D M, Maddock R J. Mapping intramuscular tenderness variation in four muscles of the beef round [J]. Journal of Animal Science, 2002, 80: 2594-2599
    [155] Wulf D M, Tatum J D, Green R D, et al. Genetic influences on beef longissimus palatability in Charolais and Limousin sired steers and heifers [J]. Journal of Animal Science, 1996, 74: 2394-2405
    [1] Cross H R, Crouse J D, MacNeil M D. Influence of breed, sex, age and electrical stimulation on carcass and palatability traits of three bovine muscles [J]. Journal of Animal Science, 1984, 58: 1358-1365.
    [2] Vestergaard M, Oksbjerg N, Henckel E Influence of feeding intensity, grazing and finishing feeding on muscle fiber characteristics and meat color of semitendinosus, longissimus dorsi and suprasinatus muscles of young bulls [J]. Meat Science, 2000, 54: 177-185.
    [3] Sami A S, Augustini C, Schwarz F J. Effects of feeding intensity and time on feed on performance, carcass characteristics and meat quality of Simmental bulls [J]. Meat Science, 2004, 67: 195-201.
    [4] Rees M P, Trout G R, Warner R D. The influence of the rate of pH decline on the rate of ageing for pork. I: interaction with method of suspension [J]. Meat Science, 2003, 65: 791-804.
    [5] Hwang I H, Devine C E, Hopkins D L. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness [J]. Meat Science, 2003, 65: 677-691.
    [6] Rees M P, Trout G R, Warner R D. The influence of the rate of pH decline on the rate of ageing for pork. II: Interaction with chilling temperature [J]. Meat Science, 2003b, 65: 805-818.
    [7] Zamora F, Aubry L, Sayd T, et al. Serine peptidase inhibitors, the best predictor of beef aging amongst a large set of quantitative variables [J]. Meat Science, 2005, 71: 730-742.
    [8] Jeremiah L E, Gibson L L. Cooking influences on the palatability of roasts from the beef hip [J]. Food Research International, 2003, 36: 1-9.
    [9] Obuz E, Dikeman M E, Loughin T M. Effects of cooking method, reheating, holding time, and holding temperature on beef longissimus lumborum and biceps femoris tenderness [J]. Meat Science, 2003, 65: 841-851.
    
    [10] Davey C L, Gilbert K V. Temperature dependent cooking toughness in beef [J]. Journal of the Science of Food and Agriculture, 1974, 25: 931-938
    [11] Martens H, Stabussvik E, Martens M. Texture and color changes in meat during cooking related to thermal denaturation of muscle proteins [J]. Journal of Texture Studies, 1982,13: 291-309.
    [12] Bouton P E, Harris P V, Ratcliff D. Effect of cooking temperature and time on the shear properties of meat [J] . Journal of Food Science, 1981, 46: 1082-1087.
    [13] Christensen M, Purslow P P, Larsen L M. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibers and perimysial connective tissue [J]. Meat Science, 2000, 55: 301-307.
    [14] Bouton P E, Harris P V. The effects of some postslaughter treatments on the mechanical properties of bovine and ovine muscle [J]. Journal of Food Science, 1972, 37: 539-543.
    [15] Wheeler T L, Shackelford S D, Koohmaraie M. Cooking and palatability traits of beef longissimus steaks cooked with a belt grill or an open hearth electric broiler [J]. Journal of Animal Science, 1998, 76: 2805-2810.
    [16] Naewbanij J O, Harrison D L, Stone M B. Roasting vs. cooking in a model system: tenderness of bull adductor muscle, conventionally chilled or electrically stimulated-hot boned [J]. Journal of Food Science, 1983, 48: 337-342
    [17] Obuz E, Dikeman M E, Grobbel J P, et al. Beef longissimus lumborum, biceps femoris, and deep pectoralis Warner-Bratzler shear force is affected differently by endpoint temperature, cooking method, and USDA quality grade [J]. Meat Science, 2004, 68: 243-248.
    [18] Renk B Z, Kanffman R G, Schaefer D M. Effect of temperature and method of cookery on the retention of intramuscular lipid in beef and pork [J] . Journal of Animal Science, 1985, 61: 876-881.
    [19] Badiani A, Nanni N, Gatta P P, et al. Nutrient content and retention in selected roasted cuts from 3-month-old ram lambs [J]. Food Chemistry, 1998, 61: 89-100.
    [20] AOAC. Official Methods of Analysis 13~(th) ed [M]. Association of Official Analytical Chemists, Washington, DC. 1980.
    [21] Hill F. The solubility of intramuscular collagen in meat animals of various ages [J]. Journal of Food Science, 1966, 31: 161-166.
    [22] Bergman I, Loxley R. Two improved and simplified methods for spectrophotometric determination of hydroxyproline [J]. Analytical Chemistry, 1963, 35: 1961-1965.
    [23] Light N, Champion A E. Characterization of muscle epimysium perimysium and endomysium collagens [J]. Biochemistry Journal, 1984, 219: 1017-1026.
    [24] Flint F O, Picketing K. Demonstration of collagen in meat products by an improved picro-sirius red polarization method [J]. The Analyst, 1984, 109: 1505-1508.
    [25] 朱荣生.生物电子显微镜技术[M] .南京农业大学实验指导.1992
    [26] 刘世新.实用生物组织学技术[M] .科学出版社,北京:2004
    [27] Heymann H, Hedrick H B, Karrasch M A, et al. Sensory and chemical characteristics of fresh pork roasts cooked to different endpoint temperatures [J]. Journal of Food Science, 1990, 55: 613-617.
    [28] Simmons S L, Carr T R, Mckeith F K. Effects of internal temperature and thickness on palatability of pork loin chops [J]. Journal of Food Science, 1985, 50: 313-315.
    [29] Aaslyng M D, Bejerholm C, Ertbjerg P, et al. Cooking loss and juiciness of pork in relation to raw meat quality and cooking procedure [J]. Food Quality and Preference, 2003, 14: 277-288
    [30] Bowers J A, Craig J A, Kropf DH, et al. Flavor, color, and other characteristics of beef longissimus muscle heated to seven internal temperatures between 55 and 85℃[J]. Journal of Food Science, 1987, 52: 533-536.
    [31] Vaudagna S R, Sanchez G, Neira M S, et al. Sous vide cooked beef muscles: effects of low temperature-long time (LT-LT) treatments on their quality characteristics and storage stability [J]. International Journal of Food Science and Technology, 2002, 37: 425-441.
    [32] Akinwunmi I, Thompson L D, Ramsay C B. Marbling, fat trim and doneness effects on sensory attributes, cooking loss and composition of cooked beef steaks [J]. Journal of Food Science, 1993,. 58: 242-244.
    [33] 周光宏主编.肉品学[M] .中国农业科技出版社,北京:1999
    [34] Offer G, Purslow P, Almond R, et al. Myofibrils and meat quality [J]. International Congress of Meat Science and Technology, pp161-168
    [35] Offer G, Restall D, Trinick J. Water holding in meat. In Bailey J. A. Recent Adv. Chem. Meat [M]. London: The Royal Society of Chemistry, 1984.
    [36] Combes S, Lepetit J, Darche B, et al. Effect of cooking temperature and cooking time on Warner-Bratzler tenderness measurement and collagen content in rabbit meat [J]. Meat Science, 2003, 66: 91-96.
    [37] Palka K. Changes in intramuscular connective tissue and collagen solubility of bovine semitendinosus muscle during retorting [J]. Meat Science, 1999, 53: 189-194.
    [38] Powell T H, Hunt M C, Dikeman M E. Enzymatic assay to determine collagen thermal denaturation and solubilization [J]. Meat Science, 2000, 54: 307-311.
    [39] Seideman S C. Methods of expressing characteristics and their relationship to meat tenderness and muscle fiber types [J]. Journal of Food Science, 1986, 51: 273-276.
    [40] Purslow P P. Intramuscular connective tissue and its role in meat quality [J]. Meat Science, 2005, 70: 435-447
    [41] Lawrie R A. The structure and growth of muscle. In: Lawrie's Meat Science (Sixth Edition) [M]. Woodhead Publishing limited, Cambridge England, 1998.
    [42] Stabursvik E, Martens H. Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry [J]. Journal of the Science of Food and Agriculture, 1980, 31: 1034-1042.
    [43] Ray E E, Berry B W, Loucks L J, et al. Influence of rate and length of cookery upon product attributes of pre- and post-rigor beef [J]. Journal of Food Science, 1983,48: 343-345,349.
    [44] Robertson J, Ratcliff D, Bouton P E, et al. Effect of cooking temperature and animal age on the shear properties of beef and buffalo meat [J] . Journal of Food Science, 1984,49: 1163-1166, 1177.
    [45] Crouse J D, Cross H R, Seideman S C. Effects of sex condition, genotype, diet and carcass electrical stimulation on the collagen content and palatability of two bovine muscles [J]. Journal of Animal Science, 1985, 60: 1228-1234.
    [46] Hall J B, Hunt M C. Collagen solubility of A-maturity bovine longissimus muscle affected by nutritional regimen [J]. Journal of Animal Science, 1982,55: 321-328.
    [47] Powell T H, Dikeman M E, Hunt M C. Tenderness and collagen composition of beef semitendinosus roasts cooked by conventional convective cooking and modeled, multistage convective cooking [J]. Meat Science, 2000,55: 421-425.
    [48] Brooks J C, Savell J W. Perimysium thickness as an indicator of beef tenderness [J]. Meat Science, 2004, 67: 329-334
    [49] Lewis G J, Purslow P P. The strength and stiffness of perimysial connective tissue isolated from cooked beef muscle [J]. Meat Science, 1989, 26: 255-269.
    [50] Lewis G J, Purslow P P, Rice A E. The effect of conditioning on the strength of perimysial connective tissue dissected from cooked meat [J]. Meat Science, 1991, 30:1-12.
    [51] Mutungi G M, Purslow P P, Warkup C. Influence of temperature, fiber diameter and conditioning on the mechanical properties of raw and cooked single muscle fibers extended to fracture [J]. Journal of the Science of Food and Agriculture, 1996, 72: 358-366.
    [52] Lawrence T E, King D A, Obuz E, et al. Evaluation of electric belt grill, forced-air convection oven, and electric broiler cookery methods for beef tenderness research [J]. Meat Science, 2001, 58: 239-246.
    [53] Hung C C, Davis E A, Gordon J, et al. Mechanisms of water loss of bovine semitendinosus muscle dry cooked from frozen state [J]. Journal of Food Science, 1978, 43:1191-1195.
    [54] Hearne L E, Penfield M P, Goertz G E. Heating effects on bovine semitendinosus: shear, muscle fiber measurements, and cooking losses [J]. Journal of Food Science, 1978,43:10-12.
    
    [55] 汪玉松等主编.现代动物生物化学(第二版)[M].中国农业科技出版社,北京:2002
    
    [56] Kopp J, Bonnet M. Stress-strain and isometric tension measurements in collagen. In A. M. Pearson, T. M. Dutson, & A. J. Baily (Eds.). Advances in Meat Research [M] vol. 4: collagen as a food. New York: Van Nostrand. 1987, ppl63-185.
    [1] 周光宏主编.肉品学[M] .中国农业科技出版社,北京:1999
    [2] Shorthose W R, Harris P V. Effect of animal age on the tenderness of selected beef muscles [J]. Journal of Food Science 1990, 55: 1-14.
    [3] McCormick R J. Extracellular modifications to muscle collagen: implications for meat quality [J]. Poultry Science 1999, 78: 785-791.
    [4] Judge M D, Aberle E D. Effects of chronological age and postmortem aging on thermal shrinkage temperature of bovine intramuscular collagen [J]. Journal of Animal Science 1982, 54: 68-71.
    [5] Volpelli L A, Valusso R, Morgante M, et al. Meat quality in male fallow deer (Dama dama): effects of age and supplementary feeding [J]. Meat Science 2003, 65: 555-562.
    [6] Fang S H, Nishimura T, Takahashi K. Relationship between development of intramuscular connective tissue and toughness of pork during growth of pigs [J]. Journal of Animal Science, 1999, 77: 120-130
    [7] Dikeman M E, Reddy G B, Arthaud V H, et al. Longissimus muscle quality, palatability and connective tissue histological characteristics of bulls and steers fed different energy levels and slaughtered at four ages [J]. Journal of Animal Science 1986, 63:92-101.
    [8] Avery N C, Sims T J, Warkup C, et al. The role of collagen in meat toughness; an assessment of the influence of metabolic age [J]. In Proceedings of the 44~(th) International Congress of Meat Science and Technology, Barcelona, Spain, 1998, pp. 720-721.
    [9] Duckett S K, Snowder G D, Cockett N E. Effect of the callipyge gene on muscle growth, calpastatin activity, and tenderness of three muscles across the growth curve [J]. Journal of Animal Science 2000, 78: 2836-2841.
    [10] USDA. United States standards for grades of carcass beef [M]. Agriculture Marketing Service, USDA, Washington, DC. 1997.
    [11] AUS-MEAT. Handbook of Australian meat (Sixth Edition) [M]. Australian Meat and Livestock Corporation, Brisbane, Queensland, Australia, 1998.
    [12] China's Ministry of Agriculture (CMA). Beef quality grading (NY/T676-2003) [M]. China's Standard Publishing, Beijing, China, 2003.
    [13] National Bureau of Statistics of China (NBSC). Precedence of main indicators of China in the world. In: International StatisticalYearbook [M]. China Statistics Press, Beijing, China, 2004, pp.226-227.
    [14] China's Academy of Agriculture (CAA). Niu pinzhong gelun. In: Zhongguo niu pinzhong zhi [M]. Shanghai Science and Technology Publishing, Shanghai, China, 1986, pp. 30-100.
    [15] Hill F. The solubility of intramuscular collagen in meat animals of various ages [J]. Journal of Food Science 1996, 31:161-166.
    [16] Bergman I., Loxley R. Two improved and simplified methods for spectrophotometric determination of hydroxyproline [J]. Analytical Chemistry'1963,35:1961-1965.
    [17] Light N, Champion A E. Characterization of muscle epimysium, perimysium and endomysium collagens [J]. Biochemistry Journal 1984,219:1017-1026.
    [18] Cross H R, West R L, Dutson T R. Comparison of methods for measuring sarcomere length in beef semitendinosus muscle [J]. Meat Science 1981,5: 261-266
    [19] Flint F O, Pickering K. Demonstration of collagen in meat products by an improved picro-sirius red polarization method [J]. The Analyst 1984,109:1505-1508.
    [20] Nishimura T, Hattori A, Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese Black Cattle, effect of marbling on beef tenderization [J]. Journal of Animal Science 1999,11: 93-104.
    [21] Cerhardy M. Quality of beef from commercial fattening systems in northern Germany [J]. Meat Science 1995,40:103-120.
    [22] Miller R K, Tatum J D, Cross H R, et al. Effects of carcass maturity on collagen solubility and palatability of beef from grain-finished steers [J]. Journal of Food Science 1983, 48: 484-486,525.
    [23] Shimokomaki M, Elsolen D F, Bailey A J. Meat tenderness: age-related changes in bovine intramuscular collagen [J]. Journal of Food Science1912,37: 892-896.
    [24] Seideman S C. Methods of expressing characteristics and their relationship to meat tenderness and muscle fiber types [J]. Journal of Food Science 1986,51: 273-276.
    [25] Smith S H, Judge M D. Relationship between pyridinoline concentration and thermal stability of bovine intramuscular collagen [J]. Journal of Animal Science 1991, 69: 1989-1993.
    [26] Sink J D, Turgut H, Mann O M, et al. Effect of age and sex on biophysical properties of fresh beef muscles from bullocks and steers [J]. Journal of Food Science 1983,48: 844-847.
    [27] Veiseth E, Shackelford S D, Wheeler T L, et al. Factors regulating lamb longissimus tenderness are affected by age at slaughter [J]. Meat Science2004,68: 635-640.
    [28] Purslow P P. Intramuscular connective tissue and its role in meat quality. Meat Science 2005, 70: 435-447.
    [29] Cross H R, Crouse J D, MacNeil M D. Influence of breed, sex, age and electrical stimulation on carcass and palatability traits of three bovine muscles [J]. Journal of Animal Science 1984, 58:1358-1365.
    [30] Wheeler T L, Shackelford S D, Koohmaraie M. Technical note: Sampling methodology for relating sarcomere length, collagen concentration, and the extent of postmortem proteolysis to beef and pork longissimus tenderness [J]. Journal of Animal Science2002, 80: 982-987.
    [31] Cooper C C, Breidenstein B B, Cassens R G, et al. Influence of marbling and maturity on the palatability of beef muscle II. Histological considerations [J]. Journal of Animal Science 1968, 27: 1542-1546.
    [32] Okeudo N J, Moss B W. Interrelationships amongst carcass and meat quality characteristics of sheep [J]. Meat Science2005, 69: 1-8.
    [1] 周光宏主编.肉品学[M] .中国农业科技出版社,北京,1999
    [2] USDA. United States standards for grades of carcass beef. Agriculture Marketing Service, USDA, Washington, DC, 1997.
    [3] AUS-MEAT. Handbook of Australian meat (6th edition) [M]. Australian Meat and Livestock Corporation, Brisbane, Queensland, Australia, 1998.
    [4] 日本食肉规格付协会.平成13年.牛·豚·枝肉·部分肉取引规格解说书.
    [5] Kyung C K. Chapter 15. Meat marketing and grading system in Korea. Available:agis.nlri.go.kr/korea/library/Book/upload/P1/B04-14.PDE Accessed: Jan 10, 2006
    [6] 中国农业部.牛肉质量分级[M] .中国标准出版社,北京,2003
    [7] Kim C J, Lee E S. Effects of quality grade on the chemical, physical and sensory characteristics of Hanwoo (Korean native cattle) beef [J]. Meat Science, 2003, 63: 397-405.
    [8] Brooks J C, Belew J B, Griffin D B, et al. National beef tenderness survey-1998 [J]. Journal of Animal Science, 2000, 78: 1852-1860.
    [9] Savell J W, Branson R E, Cross H R, et al. National consumer retail beef study: palatability evaluations of beef loin steaks that differed in marbling [J]. Journal of Food Science, 1987, 52: 517-519.
    [10] Nishimura T, Hattori A, Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese Black Cattle, effect of marbling on beef tenderization [J]. Journal of Animal Science, 1999, 77: 93-104.
    [11] Hill F. The solubility of intramuscular collagen in meat animals of various ages [J]. Journal of Food Science, 1966, 31: 161-166.
    [12] Bergman I., Loxley R. Two improved and simplified methods for spectrophotometric determination of hydroxyproline [J]. Analytical Chemistry, 1963, 35: 1961-1965.
    [13] Light N, Champion A E. Characterization of muscle epimysium perimysium and endomysium collagens [J]. Biochemistry Journal, 1984, 219: 1017-1026.
    [14] Cross H R, West R L, Dutson T R. Comparison of methods for measuring sarcomere length in beef semitendinosus muscle [J]. Meat Science, 1981, 5: 261-266.
    [15] Flint F O, Pickering K. Demonstration of collagen in meat products by an improved picro-sirius red polarization method [J]. The Analyst, 1984, 109: 1505-1508.
    [16] Savell J W, Cross H R, Smith G C. Percentage ether extractable fat and moisture content of beef longissimus muscle as related to USDA marbling score [J]. Journal of Food Science, 1986, 51: 838, 840.
    [17] Hedrick H B, Krause G F, Ellersieck M R, et al. Beef carcass composition as influenced by yield and quality grade [J]. Journal of Animal Science, 1981, 53: 102-106.
    [18] Von Seggern D D, Calkins C R, Johnson D D, et al. Muscle profiling: characterizing the muscles of the beef chuck and round [J]. Meat Science, 2005, 71: 39-51.
    [19] Romans J R, Tuma H J, Tucker W L. Influence of carcass maturity and marbling on the physical and chemical characteristics of beef. I. Palatability, fiber diameter and proximate analysis [J]. Journal of Animal Science, 1965, 24: 681-685.
    [20] Savell J W, Mueller S L, Baird B E. The chilling of carcasses [J]. Meat Science, 2005,70: 449-459.
    [21] Cooper C C, Breidenstein B B, Cassens RG,et al. Influence of marbling and maturity muscle. II. Histological considerations [J]. Journal of Animal Science, 1968, 27: 1542-1546.
    [22] Parrish F C, Olson D G, Miner B E, et al. Effect of degree of marbling and internal temperature of doneness on beef rib steaks [J]. Journal of Animal Science, 1973, 37: 430-434.
    [23] Jeremiah L E. The influence of subcutaneous fat thickness and marbling on beef, palatability and consumer acceptability [J]. Food Research International, 1996, 29: 513-520.
    [24] Ozawa S, Mitsuhashi T, Mitsumoto M, et al. The characteristics of muscle fiber types of longissimus thoracis muscle and their influences on the quantity and quality of meat from Japanese Black steers [J]. Meat Science, 2000, 54: 65-70.
    [25] Aaslyng M D, Bejerholm C, Ertbjerg P, et al. Cooking loss and juiciness of pork in relation to raw meat quality and cooking procedure [J]. Food Quality and Preference, 2003, 14: 277-288
    [26] Offer G, Purslow P, Almond R, et al. Myofibrils and meat quality [J]. International Congress of Meat Science and Technology, ppl61-168
    [27] Obuz E, Dikeman M E, Grobbel J P, et al. Beef longissimus lumborum, biceps femoris, and deep pectoralis Warner-Bratzler shear force is affected differently by endpoint temperature, cooking method, and USDA quality grade [J]. Meat Science, 2004, 68: 243-248.
    [28] Tatum J D, Smith G C, Carpenter Z L. Interrelationships between marbling, subcutaneous fat thickness and cooked beef palatability [J]. Journal of Animal Science, 1982, 54: 777-784.
    [29] Fiems L O, De Campeneere E, De Smet S, et al. Relationship between fat depots in carcasses of beef bulls and effect on meat colour and tenderness [J]. Meat Science, 2000,56: 41-47.
    [30] Luchak G L, Miller R K, Belk K E, et al. Determination of sensory, chemical and cooking characteristics of retail beef cuts differing in intramuscular and external fat [J]. Meat Science, 1998, 50: 55-72.
    [31] McBee J L, Wiles J A. Influence of marbling and carcass grade on the physical and chemical characteristics of beef [J]. Journal of Animal Science, 1967, 26: 701-704.
    [32] McKenna D R, Lorenzen C L, Pollok K D, et al. Interrelationships of breed type, USDA quality grade, cooking method, and degree of doneness on consumer evaluations of beef in Dallas and San Antonio, Texas, USA [J]. Meat Science, 2004, 66: 399-406.
    [33] Wheeler T L, Cundiff L V, Koch R M. Effects of marbling degree on beef palatability in Bos taurus and Bos indicus cattle [J]. Journal of Animal Science, 1994, 72: 3145-3515.
    [34] Bratcher C L, Johnson D D, Littell R C, et al. The effects of quality grade, aging, and location within muscle on Warner-Bratzler shear force in beef muscles of locomotion [J]. Meat Science, 2005, 70: 279-284.
    [35] Riley D G, Johnson D D, Chase C C, et al. Factors influencing tenderness in steaks from Brahman cattle [J]. Meat Science, 2005, 70: 347-356
    [36] Denoyelle C, Lebihan E. Intramuscular variation in beef tenderness [J]. Meat Science, 2004, 66: 241-247.
    [37] Shackelford S D, Wheeler T L, Koohmaraie M. Repeatability of tenderness measurements in beef round muscles [J]. Journal of Animal Science, 1997, 75: 2411-2416.
    [38] Reuter B J, Wulf D M, Maddock R J. Mapping intramuscular tenderness variation in four major muscles of the beef round [J]. Journal of Animal Science, 2002, 80: 2594-2599.
    [39] Swanson L A, Kline E A, Goll D E. Variability of muscle fiber size in bovine longissimus dorsi [J]. Journal of Animal Science, 1965, 24: 97-101.
    [40] Janz J A M, Aalhus J L, Dugan M E R, et al. A mapping method for the description of Warner-Bratzler shear force gradients in beef longissimus thoracis et lumborum and semitendinosus [J]. Meat Science, 2006,72:79-90.
    [41] Fortin A, Robertson W M, Tong A K W. The eating quality of Canadian pork and its relationship with intramuscular fat [J]. Meat Science, 2005,69: 297-305.
    [42] Jones B K, Tatum J D. Predictors of beef tenderness among carcasses produced under commercial conditions [J]. Journal of Animal Science, 1994,72:1492-1501.
    [43] Renand G, Picard B, Touraille C, et al. Relationship between muscle characteristics and meat quality traits of young Charolais bulls [J]. Meat Science, 2001,59:49-60.
    [1] Brooks J C, Belew J B, Griffin B D, et al. National beef tenderness survey-1998 [J]. Journal of Animal Science, 2000, 78: 1852-1860.
    [2] Nishimura T, Liu A, Hattori S, et al. Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef [J]. Journal of Animal Science, 1998, 76: 528-532.
    [3] Geesink G H, Koolmees P A, van Laack H L J M, et al. Determinants of tenderization in beef Longissimus dorsi and Triceps brachii muscles [J]. Meat Science, 1995, 41: 7-17.
    [4] Jung S, Ghoul M, de Lamballerie-Anton M. Changes in lysosomal enzyme activities and shear values of high pressure treated meat during aging [J]. Meat Science, 2000, 56: 239-246.
    [5] Koohmaraie M. Biochemical factors regulating the toughening and tenderization processes of meat [J]. Meat Science, 1996, 43: S193-S201.
    [6] Takahashi K. Structural weakening of skeletal muscle tissue during post-mortem aging of meat: the non-enzymatic mechanism of meat tenderization [J]. Meat Science, 1996, 43: S67-S80.
    [7] Liu A, Nishimura T, Takahashi K. Structural weakening of intramuscular connective tissue during postmortem aging of chicken semitendinosus muscle [J]. Meat Science, 1995, 39: 135-142.
    [8] Nishimura T, Hattori A, Takahashi K. Structural weakening of intramuscular connective tissue during conditioning of beef [J]. Meat Science, 1995, 39: 127-133.
    [9] 国家统计局.统计年鉴2005[M] .统计出版社,北京,2005.
    [10] 中国农科院.中国牛品种志[M] .上海科技出版社,上海,1986.
    [11] 黄明,周光宏等.不同日两水平和成熟时间对牛肉食用品质的影响[J] .南京农业大学学报,2003.26:93-96.
    [12] AOAC. Official Methods of Analysis (Thirteen Edition) [M]. Association of Official Analytical Chemists, Washington, DC, 1980.
    [13] Hill E The solubility of intramuscular collagen in meat animals of various ages [J]. Journal of Food Science, 1966, 31: 161-166.
    [14] Bergman I, Loxley R. Two improved and simplified methods for spectrophotometric determination of hydroxyproline [J]. Analytical Chemistry, 1963, 35: 1961-1965.
    [15] Light N, Champion A E. Characterization of muscle epimysium perimysium and endomysium collagens [J]. Biochemistry Journal, 1984, 219: 1017-1026.
    [16] Flint F O, Pickering K. Demonstration of collagen in meat products by an improved picro-Sirius red polarization method [J]. The Analyst, 1984, 109: 1505-1508.
    [17] Nishimura T, Hattori A, Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese Black Cattle, effect of marbling on beef tenderization [J]. Journal of Animal Science, 1999, 77: 93-104.
    [18] Boakye K, Mittal G S. Changes in pH and water holding properties of is longissimus dorsi muscle during beef aging [J]. Meat Science, 1993, 34: 335-349.
    [19] Joo S T, Kauffman R G, van Laack R L J M, et al. Variations in rate of water loss as related to different types of post-rigor porcine musculature during storage [J]. Food Chemistry and Toxicology, 1999, 5: 865-868.
    [20] Kristensen L, Purslow P. The effect of aging on the water-holding capacity of pork: role of cytoskeletal proteins [J]. Meat Science, 2001, 58: 17-23.
    [21] Bertram H C, Whittaker A K, Shorthose W R, et al. Water characteristics in cooked beef as influenced by aging and high-pressure treatment-an NMR micro image study [J]. Meat Science, 2004, 66: 301-306.
    [22] George-Evins C D, Unruh J A, Waylan A T, et al. Influence of quality classification, aging period, blade tenderization, and endpoint cooking temperature on cooking characteristics and tenderness of beef gluteus medius steaks [J]. Journal of Animal Science, 2004, 82: 1863-1867.
    [23] Warris P D, Brown S N. The relationships between initial pH, reflectance and exudation in pig muscle [J]. Meat Science, 1987, 20: 65-74.
    [24] Mitchell G E, Giles J E, Rogers S A, et al. Tenderizing, aging, and thawing effects on sensory, chemical and physical properties of beef steaks [J]. Journal of Food Science, 1991, 56: 1125-1129.
    [25] Palka K. The influence of postmortem aging and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle [J]. Meat Science, 2003, 64:191-198.
    [26] Jeremiah L E, Gibson L L. The effects of postmortem product handling and aging time on beef palatability [J]. Food Research International, 2003, 36: 929-941.
    [27] Parrish F C, Rust R E, Popenhagen G R, et al. Effect of postmortem aging time and temperature on beef muscle attributes [J]. Journal of Animal Science, 1969, 29: 398-403.
    [28] Whipple G, Koohmaraie M, Dikeman M E, et al. Predicting beef longissimus tenderness from various biochemical and histological muscle traits [J]. Journal of Animal Science, 1990, 68: 4193-4199.
    [29] Nishimura T, Hattori A, Takahashi K. Relationship between degradation of proteoglycans and weakening of the intramuscular connective tissue during postmortem aging of beef [J]. Meat Science, 1996,42: 251-260.
    [30] Purslow P P. Intramuscular connective tissue and its role in meat quality. Meat Science, 2005, 70: 435-447.
    [31] Findlay C J, Parkin K L, Stanley D W. Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins. Journal of Food Biochemistry, 1986,10:1-15.
    [32] Findlay C J, Stanley D W. Differential scanning calorimetry of beef muscle: influence of postmortem conditioning [J]. Journal of Food Science, 1984, 49:1513-1516.
    [33] Monson F, Sanudo C, Sierra I. Influence of cattle breed and aging time on textural meat quality [J]. Meat Science, 2004, 68: 595-602.
    [34] Martinez-Cerezo S, Sanudo C, Panea B, et al. Breed, slaughter weight and aging time on consumer appraisal of three muscles of lamb [J]. Meat Science, 2005, 69: 797-805.
    [35] Sanudo C, Made E S, Olleta J L, et al. The effects of slaughter weight, breed type and aging time on beef meat quality using two different texture devices [J]. Meat Science, 2004,66: 925-932
    [36] Bruce H L, Stark J L, Beilken S L. The effects of finishing diet and postmortem aging on the eating quality of the m. longissimus thoracis of electrically stimulated Brahman steer carcass [J]. Meat Science, 2004,67: 261-268.
    [37] Bowles A J E, Kastner C L, Dikeman M E, et al. Effects of beef carcass electrical stimulation, hot boning, and aging on unfrozen and frozen longissimus dorsi, and semimembranosus steaks [J]. Journal of Food Science, 1983, 48: 332-336.
    [38] Braghieri A, Gifuni G F, Girolami A, et al. Chemical, physical and sensory properties of meat from pure and crossbred Podolian bulls at different aging times [J]. Meat Science, 2005, 69: 681-689.
    [39] Boleman C T, McKenna D R, Ramsey W S, et al. Influence of feeding vitamin D_3 and aging on the tenderness of four lamb muscles [J]. Meat Science, 2004,67:185-190.
    [40] Xie Y R, Busboom J R, Cornforth D P, et al. Effects of time on feed and postmortem aging on palatability and lipid composition of crossbred Wagyu beef [J]. Meat Science, 1996, 43: 157-166.
    [41] Bratcher C L, Johnson D D, Littell R C, et al. The effects of quality grade, aging, and location within muscle on Warner-Bratzler shear force in beef muscles of locomotion [J]. Meat Science, 2005, 70: 279-284.
    [42] Harris J J, Miller R K, Savell J W, et al. Evaluation of the tenderness of beef top sirloin steaks [J]. Journal of Food Science, 1992, 57: 6-9,15.
    [43] Kolczak T, Pospiech E, Palka K, et al. Changes of myofibrillar and centrigual drip proteins and shear force of psoas major and minor and semitendinosus muscles from calves, heifers and cows during post-mortem aging [J]. Meat Science, 2003, 64: 69-75.
    [44] 黄明.牛肉成熟机制及食用品质研究[D] .南京农业大学博士论文,2003
    [45] Lamare M, Taylor R G., Farout L, et al. Changes in proteasome activity during postmortem aging of bovine muscle [J]. Meat Science, 2002, 61: 199-204
    [46] Goll D E. Role of proteinases and protein turnover in muscle growth and meat quality [J]. Reciprocal Meat Conference Proceedings, 1991, 44: 25-36.
    [47] Stanton C, Light N. The effects of conditioning on meat collagen: Part 3. Evidence of proteolytic damage to endomysial collagen after conditioning [J]. Meat Science, 1990, 27: 41-54.
    [1] Sacks M S, Kronick P L, Buechler P R. Contribution of intramuscular connective tissue to the viscoelastic properties of post-rigor bovine muscle [J]. Journal of Food Science, 1988, 53: 19-24.
    [2] Denoyelle C, Lebihan E. Intramuscular variation in beef tenderness [J]. Meat Science, 2004, 66: 241-247.
    [3] Zamora F, Aubry L, Sayd T, et al. Serine peptidase inhibitors, the best predictor of beef aging amongst a large set of quantitative variables [J]. Meat Science, 2005, 71: 730-742.
    [4] Herring H K, Cassens R G, Briskey E J. Further studies on bovine muscle tenderness as influenced by carcass position, sarcomere length, and fiber diameter [J]. Journal of Food Science, 30, 1965, 1049-1054.
    [5] Herring H K, Cassens R G, Briskey E J. Factors affecting collagen solubility in bovine muscles [J]. Journal of Food Science, 1967, 32: 534-538.
    [6] Rhee M S, Wheeler T L, Shackelford S D, et al. Variation in palatability and biochemical traits within and among eleven beef muscles [J]. Journal of Animal Science, 2004, 82: 534-550.
    [7] Torrescano G, Sanchez-Escalante A, Gimenez B, et al. Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics [J]. Meat Science, 2003, 64: 85-91.
    [8] Carmack C F, Kastner C L, Dikeman M E, et al. Sensory evaluation of beef-flavor-intensity, tenderness, and juiciness among major muscles [J]. Meat Science, 1995,39:143-147.
    [9] Seideman S C. Methods of expressing characteristics and their relationship to meat tenderness and muscle fiber types [J]. Journal of Food Science, 1986,51: 273-276
    [10] Mckeith F K, DeVol D L, Miles R S, et al. Chemical and sensory properties of thirteen major beef muscles [J]. Journal of Food Science, 1985,50:869-872.
    [11] Shackelford S D, Wheeler T L, Koohmaraie M. Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle [J]. Journal of Animal Science, 1995, 73:3333-3340
    [12] AOAC. Official Methods of Analysis (Thirteen Edition) [M]. Association of Official Analytical Chemists, Washington, DC, 1980.
    [13] Hill F. The solubility of intramuscular collagen in meat animals of various ages [J]. Journal of Food Science, 1966,31:161-166.
    [14] Bergman I, Loxley R. Two improved and simplified methods for spectrophotometric determination of hydroxyproline [J]. Analytical Chemistry, 1963, 35:1961-1965.
    [15] Light N, Champion A E. Characterization of muscle epimysium perimysium and endomysium collagens [J]. Biochemistry Journal, 1984, 219:1017-1026.
    [16] Flint F O, Pickering K. Demonstration of collagen in meat products by an improved picro-sirius red polarization method [J]. The Analyst, 1984,109:1505-1508.
    [17] Nishimura T, Hattori A, Takahashi K. Structural changes in intramuscular connective tissue during the fattening of Japanese Black Cattle, effect of marbling on beef tenderization [J]. Journal of Animal Science, 1999,77: 93-104
    [18] Hawrysh Z J, Gifford S R, Price M A. Cooking and eating quality characteristics of dark-cutting beef from young bulls [J]. Journal of Animal Science, 1985,60: 682-690.
    [19] Jeremiah L E, Dugan M E R, Aalhus J L, et al. Assessment of the chemical and cooking properties of the major beef muscles and muscle groups [J]. Meat Science, 2003,65:985-992.
    [20] Von Seggern D D, Calkins C R, Johnson D D, et al. Muscle profiling: Characterizing the muscles of the beef chuck and round [J]. Meat Science, 2005,71: 39-51.
    [21] Lawrie R A. The structure and growth of muscle. In: Lawrie's Meat Science (Sixth Edition) [M]. Woodhead Publishing limited, Cambridge England, 1998.
    [22] Aaslyng M D, Bejerholm C, Ertbjerg P, et al. Cooking loss and juiciness of pork in relation to raw meat quality and cooking procedure [J]. Food Quality and Preference, 2003,14: 277-288.
    [23] Vestergaard M, Therkisen M, Henckel P, et al. Influence of feeding intensity, grazing, and finishing feeding on meat and eating quality of young bulls and the relationship between muscle fiber characteristics, fiber fragmentation and meat tenderness [J]. Meat Science, 2000,54:187-195.
    [24] Vestergaard M, Oksbjerg N, Henickel P. Influence of feeding intensity, grazing and finishing feeding on muscle fiber characteristics and meat color of seraitendinosus, longissimus dorsi and suprasinatus muscles of young bulls [J]. Meat Science, 2000, 54: 177-185.
    [25] Gerrard D E, Jones S J, Aberle E D, et al. Collagen stability, testosterone secretion and meat tenderness in growing bulls and steers [J]. Journal of Animal Science, 1987, 65: 1236-1242.
    [26] Findlay C J, Parkin K L, Stanley D W. Differential scanning calorimetry can determine kinetics of thermal denatura tion of beef muscle proteins [J]. Journal of Food Biochemistry, 1986, 10: 1-15.
    [27] Judge M D, Aberle E D. Effect of chronological and postmortem aging on thermal shrinkage temperature of bovine intramuscular collagen [J]. Journal of Animal Science, 1982, 54: 68-71
    [28] Nishimura T., Hattori A., Takahashi K. Relationship between degradation of proteglycans and weakening of the intramuscular connective tissue during postmortem ageing of beef [J]. Meat Science, 1996, 42: 251-260
    [29] 周光宏主编.肉品学[M] .中国农业科技出版社,北京,1999.
    [30] Janz J A M, Aalhus J L, Dugan M E R, et al. A mapping method for the description of Warner-Bratzler shear force gradients in beef longissimus thoracis et lumborum and semitendinosus [J]. Meat Science, 2006, 72: 79-90.
    [31] 黄明,周光宏等.未育肥黄牛的产肉性能与牛肉食用品质的研究[J] .食品科学,2002,23(9):33-36
    [32] Boyer-Berri B, Greaser M L. Effect of postmortem storage on the Z-line region of titin in bovine muscle [J]. Journal of Animal Science, 1998, 76: 1034-1044.
    [33] Hwang I H, Park B Y, Cho S H, et al. Effects of muscle shortening and proteolysis on Warner-Bratzler shear force in beef longissimus and semitendinosus [J]. Meat Science, 2004, 68: 497-505.
    [34] Klastrup S, Cross H R, Schanbacher B D, et al. Effects of castration and electrical stimulation on beef carcass quality and palatability characteristics [J]. Journal of Animal Science, 1984, 58: 75-84.
    [35] Burson D E, Hunt M C. Proportion of collagen type Ⅰ and Ⅲ in four bovine muscles differing in tenderness [J]. Journal of Food Science, 1986, 51: 51-53.
    [36] Jeremiah L E, Dugan M E R, Aalhus J L, et al. Assessment of the relationship between chemical components and palatability of major beef muscles and muscle groups [J]. Meat Science, 2003, 65: 1013-1019.
    [37] Riley D G, Johnson D D, Chase C C, et al. Factors influencing tenderness in steaks from Brahman cattle [J]. Meat Science, 2005, 70: 347-356.
    [38] Morgan J B, Wheeler T L, Koohmaraie M, et al. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers [J]. Journal of Animal Science, 1993, 71: 1471-1477
    [39] Herring H K, Cassens R G, Suess G G, et al. Tenderness and associated characteristics of stretched and contracted bovine muscle [J]. Journal of Food Science, 1967, 32: 317-323
    [40] Lewis P K, Brown C J, Heck M C. Fiber diameter, sarcomere length and tenderness of certain muscles of crossbred beef steers [J]. Journal of Animal Science, 1977, 45: 254-260

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700