摘要
淀粉是成熟小麦籽粒的主要组成成分,约占小麦籽粒重量的65%左右,由分支很少的直链淀粉和高度分支的支链淀粉两种葡萄糖多聚体组成。直链淀粉与支链淀粉的比例(直/支比)影响淀粉的理化性质和黏滞性谱(RVA谱)特性,进而影响小麦的加工品质、食用品质和工业用途。然而直链淀粉含量相同或相近的品种之间,淀粉品质却表现出明显差异,说明除直/支比外,支链淀粉的精细结构如聚合度、分支化度、链长分布和平均链长等结构参数也显著影响小麦品质。淀粉分支酶(SBE)是唯一引入α–1,6糖苷分支键的淀粉合成酶,因此SBE的性质和活性是影响支链淀粉精细结构和含量的重要因素。本研究选用种源地分布有代表性的90个小麦品种为材料,应用非变性聚丙烯酰胺凝胶电泳(Native–PAGE)和SDS–聚丙烯酰胺凝胶电泳(SDS–PAGE)检测了淀粉分支酶同工酶的等位基因分布特点和基因型组成,鉴定了SBE各同工酶的遗传多态性,研究了SBE等位基因位点和基因型与酶活性的关系,分析了SBE等位基因位点和基因型对支链淀粉含量的遗传效应,以期为阐明小麦淀粉品质形成的分子机制和小麦淀品质改良提供理论依据,主要研究结果如下。
1.胚乳可溶性基质SBE遗传多样性鉴定
应用Native–PAGE检测表明,SBE有SBEⅠ和SBEⅡ两种同种型,SBEⅠ同种型表现丰富多态性,具有A、Dⅰ、Dⅱ和B 4个基因位点,其出现频率分别为22.2%、98.9%、48.9%和75.6%。而SBEⅡ同种型只具有SBEⅡa单一基因位点,未显现多态性。在所有测试品种中,共检测到7种基因型, Dⅰ基因位点几乎出现在所有基因型中,对基因型组成的贡献率最大;D与B位点组成的基因型(DⅰB和DⅰDⅱB)的出现频率高于与A位点组成的基因型(ADⅰB和ADⅰDⅱ);每一个基因型(品种)只有4个基因位点的1～3个,未检测到具有4个基因位点的基因型。
2. SBE两种同种型酶活性分析
应用Nagamine等文献中的方法在Native–PAGE凝胶上对SBE进行酶活性染色,并通过降低酶活性染色的协同酶–磷酸化酶的浓度,对SBE两种同种型酶活性进行分析,结果在凝胶上只显现SBEⅡ酶带,但SBEⅠ酶带未显现,表明SBEⅡ活性大于SBEⅠ。
3. SBEⅡb亚细胞定位及表达分析
SBEⅡb在小麦籽粒发育的早期开始表达,但表达量较低,从花后14d至28d其表达量几乎恒定不变。不同发育时期SBEⅡb的活性有差异,其酶活性表达高峰出现在花后第21d左右。在籽粒发育后期,SBEⅡb被淀粉粒所包裹,成为淀粉粒结合蛋白,暂时丧失活性,一旦淀粉粒结构遭到破坏释放SBEⅡb,其活性立即恢复。SDS–PAGE检测表明,所有被试品种都具有单一SBEⅡb位点,表明SBEⅡb不具有遗传多样性。
4. SBE基因型与酶活性的关系
统计分析SBE各个基因位点和基因型的酶活性并进行差异显著性测验和多重比较。单一基因位点分析表明:A、Dⅰ、Dⅱ和B 4个基因位点的酶活性之间差异达极显著水平(p<0.01),其中A基因位点所表达的酶活性最高,而其它3个基因位点之间差异未达到显著水平;基因型分析表明:由A位点组成的基因型酶活性最高,与不含A位点的基因型相比差异达显著水平(p<0.05),而缺乏A位点的基因型之间酶活性无显著差异(p<0.05)。由于SBEⅡ同种型不具有多态性,因此SBE酶活性与SBEⅠ具有显著相关性,与SBEⅡ相关性不显著,其中A基因位点或含有A位点的基因型对酶活性的影响最大。
5. SBE基因型对支链淀粉含量遗传效应分析
单一基因位点的分析结果表明:A基因位点的支链淀粉含量最高,Dⅰ位点最低,在0.01水平上差异显著;多个等基因位点(基因型)的联合效应分析表明,组成基因型的基因位点越多,支链淀粉含量越高,与酶活性分析结果呈完全一致的趋势。其中,含有A基因位点的基因型(ADⅰDⅱ和ADⅰB)所对应的支链淀粉含量较高,与不含A位点的基因型(DⅰB、DⅰDⅱ和Dⅰ)的支链淀粉含量差异达显著水平(P<0.05)。SBE不同基因型对支链淀粉生物合成具有不同的遗传效应,显著影响支链淀粉含量;而且A基因位点和含有A基因位点的基因型遗传效应最大,可为筛选不同支链淀粉含量的小麦品种及淀粉品质改良提供参考。
Strach is the major component of wheat grain, accounting for about 65% of the final dry weight of grain, and is composed of two distinct types of glucose polymer; amylose, which makes up 22～26% of normal starch, is an essentially linear molecule in which the glucose units are joined byα–1, 4 linkages, amylopectin is a much larger branched glucan polymer typically constituting 74～78% of the starch mass, produced by the formation ofα–1, 6 linkages between adjoining straight glucan chains. It is generally held that the ratio of amylose and amylopectin is a major determinant for physiochemical characteristics and Rapid Viso–analyzer(RVA) profile of starch, further influencing processing, cooking and eating qualities of wheat. However, previous studies also showed that there were significant differences in wheat quality among the varieties with similar amylose content. It is infered that fine structure of amylopectin, e.g. degree of polymerization, degree of branching, average chain length and chains distribution, also played an important role in wheat quality. Starch branching enzyme(SBE) is a sole enzyme to introduce branching points in the amylopectin molecules. Therefore the properties and activities of SBE are responsible for amylopectin structure.
In order to elucidate the molecular mechanism of wheat quality and provide theoretical base for improving the quality of wheat starch, Ninety wheat cultivars from different provenances were used in the present study, including some typical hexaploid wheat from various province of China and some high–yielding modern varieties as well as exotic ones. The gene loci, genotypes and genetic diversity of SBE isozymes were determined by using native and SDS polyacrylamide gel electrophoresis (Native–PAGE and SDS–PAGE). The correlation between isozyme genotypes and enzyme activities of SBE was investigated. The genetic effects analysis were made for isozyme genotypes of SBE on amylopectin content. The main results were as follows.
1. Genetic diversity of SBE in soluble stroma of endosperm
The genetic diversity of SBE was characterized through Native–PAGE. The result showed that there were two SBE isoforms, ie. SBEⅠand SBEⅡ. SBEⅡisoform failed to exhibit genetic polymorphism but SBEⅠmanifested genetic diversity. Four gene loci, A, B, Dⅰand Dⅱ, were identified at SBEⅠlocus, with frequency 22.2%, 98.9%, 48.9% and 75.6%, respectively. Seven genotypes were determined, and Dⅰlocus was included almost in all genotypes, which was the most contribution to genotypes formation. The frequency of genotypes comprised by D and B locus was higher than that by D and A. Each genotype was composed of the one to three gene locus among four ones. The genotype constituted by four gene locus was not observed.
2. Activity analysis of SBE isoforms
In this study, we conducted activity staining of SBE using Nagamine’s literature method in Native–PAGE gel. The result demonstrated that if phosphorylase concentration, which acted as co–working enzyme SBE activity staining, was lowered, the sole SBEⅡa but no SBEⅠzymogram was observed, indicating that SBEⅡactivity is higher than that of SBEⅠ.
3. Subcellular localization and expression level of starch granule–bound SBEⅡb
SBEⅡb expressed at the early stage during wheat grain development, and kept constant from 14th to 28th day post anthesis. There was different expression level of SBEⅡb in term of protein amount in different period of developing wheat grain, and its activity reached the maximum at the 21th day after anthesis. SBEⅡb was entraped into granule in the late period of developing grain, temporarily lossing enzyme activity. Once SBEⅡb was released from within granule by mechanical and chemical methods, the activity was recovered immediately. SDS–PAGE was conducted to examine SBEⅡb diversity. The result indicated that all cultivars tested had SBEⅡb locus, and there was no differences of the electrophoresis profile among cultivars. Therefore, similar to SBEⅡa, SBEⅡb was not of genetic polymorphism.
4. Correlation between isozyme genotypes and activity of SBE
In order to explore the relationship between the isozyme genotypes and enzyme activity of SBE, enzyme activity statistics corresponding to gene loci and genotypes was made, and multiple comparison analysis conducted. The result indicated that from single gene locus analysis, there were significant differences of the enzyme activity among A, B, Dⅰand Dⅱlocus (p<0.01), which the activity of A locus was the highest, and the one of remaining three locus had no significant differences. From genotype analysis, the activity of genotypes constituted by A and B or by A and D was the highest and exhibited a statistically significant level compared to other genotypes (p<0.05). But there was no significant differences between genotypes without A locus (p<0.05). Consequently, SBE activity correlated to SBEⅠisoform, but no significant correlation to SBEⅡwas observed. Furthermore, the effects of A gene locus and genotypes comprised by A locus on SBE activity was the most significant.
5. Genetic effects of isozyme genotypes of SBE on amylopectin content
From single gene locus analysis, amylopectin content of A locus was the highest, and the lowest for Dⅰ, which showed a statistically significant differences at 0.01 level. From joint effects analysis of multiple locus, the more gene loci constituting SBE genotypes, the more significant effects of the genotypes on amylopectin content, representing same scenario as enzyme activity analysis. Amylopectin content of genotypes containing A locus ( A DⅰDⅱand ADⅰB ) were the highest, which there was significant differences at 0.05 level compared to that of genotypes of DⅰB and DⅰDⅱ, especially to Dⅰ. There is different genetic effects for different genotypes of SBE on amylopectin content, and SBEⅠisoform plays a major role in determining amylopectin content. The effects of genotypes containing A locus is the most significant, which can provide theoretical base for the breeding and improving of wheat quality.
引文
[1]陈刚,王忠,刘巧泉,熊飞,顾蕴洁,顾国俊。转反义Wx基因水稻颖果中淀粉合成和积累相关酶活性的变化。植物生理与分子生物学学报,2006,32:209–216
[2]付崇允,李仕贵。稻米品质的分子水平研究进展。中国生物工程杂志,2003,11:28–32
[3]高振宇,黄大年。植物支链淀粉合成的关键酶。生物工程进展,1998,18:29–31
[4]高振宇,黄大年,钱前。植物支链淀粉生物合成研究进展。植物生理与分子生物学学报,2004,30:489–495
[5]何照范。粮油籽粒品质及其分析技术[M]。北京:中国农业出版社,1985,pp:144–294
[6]金善宝。中国小麦学[M]。北京:中国农业出版社,1996
[7]李太贵,沈波,陈能,罗玉坤(1997)。Q酶对水稻籽粒垩白形成的影响。作物学报,23 (3): 338–344
[8]沈波,庄杰云,樊叶杨,应杰政,杨娟,孙利香,费冀慧,郑康乐。水稻籽粒淀粉分支酶活性遗传分析。植物生理与分子生物学学报,2005,30(5):489–495
[9]盛婧,郭文善,胡宏,朱新开,封超年,彭永欣。小麦淀粉合成关键酶活性及其与淀粉积累的关系。扬州大学学报(农业与生命科学版)。2003,24 (4):49–53
[10]徐军望,李旭刚,朱祯。基因工程改良淀粉品质。生物技术通报。2000,1:10–19
[11]严长杰,田舜,张正球,韩月澎,陈峰,李欣,顾铭洪。水稻栽培品种淀粉合成相关基因来源及其对品种的影响。中国农业科学,2005,39:865–871
[12]张峰,蒋德安,翁晓燕。淀粉合酶的酶学与分子生物学研究进展。植物学通报,2001,18:177–182
[13]翟风林。作物品质育种[M]。北京:农业出版社,1991,pp:110–119
[14]张红伟,谭振波,陈荣军,李建生,陈刚。玉米淀粉生物合成及其遗传操控。遗传,2003,25:455–460
[15]姚新灵,丁向真,陈彦云,吴晓玲,郭蔼光。淀粉分支酶和去分支酶编码基因的功能。植物生理学通讯,2005,41:253–259
[16] Baba T, Nishiara M, Mizuno K, Kawasaki T, Shimada H, Kobayashi E, Ohnishi S, Tanaka K, Arai Y. Identification, cDNA cloning, and gene expression of soluble starch synthase in rice (Oryza sativa L. ) immature seeds. Plant physiol, 1993, 103: 565–573
[17] Baga M, Glaze S, Mallard C S, Chibbar R. A starch branching enzyme gene in wheat produces alternatively spliced transcripts. Plant Mol Biol, 1999, 40: 1019–1030
[18] Baga M, Nair R B, Repellin A, Scoles G J, Chibbar R N. Isolation of a cDNA encoding a granule–bound 152–kilodalton starch–branching enzyme in wheat. Plant physiol, 2000, 124: 255–263
[19] Baldwin P and France A. Starch granule–associated proteins and polypeptides: a review. Starch, 2001, 53: 475–503
[20] Ball S G, Guan H P, James M, Myers A, Keeling P, Mouille G, Buleon A, Colonna P, Preiss J. From glycogen to amylopectin: a model for the biogenesis of the plant starch granule. Cell, 1996, 86: 349–352
[21] Ball S G and Morell M K. From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu. Rev. Plant Biol, 2003, 54: 207–233
[23] Ball S G, van de Wal M H B J, Visser R G F. Progress in understanding the biosynthesis of amylose. Trends in Plant Science, 1998, 3: 462–467
[24] Beatty M K, Rahman A, Cao H, Woodman W, Lee M, Myers A M, James M G. Purification and molecular genetic characterization of ZPU1, a pullulanase–type starch debranching enzyme from maize. Plant Physiology, 1999, 119: 255–256
[25] Blauth S L, Yao Y, Klucinec J D, Shannon J C, Thompson D B, Guiltinan M. Identification of mutator insertional mutants of starch–branching enzyme 2a in corn. Plant physiol, 2001, 125: 1396–1405
[26] Blauth S L, Kim K N, Klucinec J, Shannon J C, Thompson D, Guiltinan M. Identification of mutator insertional mutants of strach–branching enzymeⅠ(sbe1) in zea mays L. Plant Mol Biol, 2002, 48: 287–297
[27] Blennow A, Engelsen S B, Nielsen T H, Baunsgaard L, Mikkelsen R. Starch phosphorylation: a new front line in starch research. Trends in Plant Science, 2002, 7: 445–450
[28] Boyer C D, Preiss J. Properties of citrate–stimulated starch synthesis catalyzed by starch synthase I of developing maize kernels. Plant Physiol, 1979, 64: 1039–1042
[29] Bresolin N C, Li Z, Kosar–Hashemi B, Tetlow I J, Chatterjee M, Rahman S, Morell M K, Howitt C A. Characterization of disproportionating enzyme from wheat endosperm. Planta, 2005, 224: 20–31
[30] Buleon A, Colonna P, Planchot V, Ball S. Starch granules: structure and biosynthesis. International Journal of Biological Macromolecules, 1998, 23 (2): 85–112
[31] Buleon A, Gallant D J, Bouchet B, Mouille G, D’Hulst C, Kossmann J, Ball S. Starches from A to C. Plant Physiol, 1997, 115: 949–957
[32] Burton R A, Bewlev J D, Smith A M. starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development. The Plant Journal, 1995, 7(1): 3–15
[33] Burton R A, Jenner H, Carrangis L, Fahy B, Fincher G B, Hylton C, Laurie D A, Parker M, Waite D, Wegan S, Verhoeven T, Denyer K. Starch granule initiation and growth are altered in barley mutants that lack isoamylase activity. The Plant Journal, 2002, 31: 97–112
[34] Bustos R, Fahy B, Hylton C M, Seale R, Nebane N M, Edwards A, Martin C, Smith A M. Starch granule initiation is controlled by a heteromultimeric isoamylase in potato tubers. Proceedings of the National Academy of Sciences USA, 2004, 101: 2215–2220
[35] Cao H and Preiss J. Evidence for essential arginine residues at the active sites of maize branching enzymes. Journal of Protein Chemistry, 1996, 15 (3): 291–304
[36] Cao H, Imparl–Radosevich J, Guan H, Keeling P L, James M G, Myers A M. Identification of the soluble starch synthase activities of maize endosperm. Plant Physiol, 1999, 120: 205–215
[37] Cao H, James M G, Myers, A M. Purification and characterization of soluble starch synthases from maize endosperm. Arch. Biochem. Biophys, 2000, 373: 135–146
[38] Colleoni C, Dauvillee D, Mouille G, Buleon A, Gallant D, Bouchet B, Morell M, Samuel M, Delrue B, d’Hulst C, Bliard C, Nuzillard J M, Ball S. Genetic and biochemical evidence for the involvement ofα–1, 4 glucanotrsferases in amylopectin synthesis. Plant Physiol, 1999, 120: 993–1003
[39] Colleoni C, Dauvillée D, Mouille G, Morell M K, Samuel M, Slomiany M C, Lie′nard L, Wattebled F, d’Hulst C, Ball S. Biochemical characterization of the Chlamydomonas reinhardtiiα–1,4 glucanotransferase supports a direct function in amylopectin biosynthesis. Plant Physiology, 1999, 120: 1005–1014
[40] Colleoni C, Myers A M, James M G. One–and two–dimensional native PAGE activity gel analyses of maize endosperm proteins reveal functional interactions between specific starch metabolizing enzymes. J. Appl. Glycosci, 2003, 50: 207–212
[41] Commuri P D and Keeling P G. chain–length specificities of maize starch synthaseⅠenzyme: studies of glucan affinity and catalytic properties. Plant J, 2001, 25: 475–486
[42] Craig J, Lloyd J R, Tomlinson K, Barber L, Edwards A, Wang T L, Martin C, Hedley C L, Smith A M. Mutations in the gene encoding starch synthaseⅡprofoundly alter amylopectin structure in pea embryos. The Plant Cell, 1998, 10: 413–426
[43] Davis B J. Disc electrophoresisⅡ: Method and application of human serum proteins. Ann NY Acad Sci, 1964, 121: 404–427
[44] Davis J P, Supatcharee N, Khandelwal R L, Chibbar R N. Synthesis of novel starches in planta: opportunities and challenges. Starch, 2003, 55: 107–120
[45] Delatte T, Trevisan M, Parker M L, Zeeman S C. Arabidopsis mutants Atisa1 and Atisa2 have identical phenotypes and lack the same multimeric isoamylase, which influences the branch point distribution of amylopectin during starch synthesis. Plant J, 2005, 41(6): 815–830
[46] Delvalle D, Dumez S, Wattebled F, Roldan I, PlanchotV, Berbezy P, Colonna P, Vyas D, Chatterjee M, Ball S, Merida A, D’Hulst C. Soluble starch synthaseⅠ: a major determinant for the synthesis of amylopectin in Arabidopsis thaliana leaves. The Plant Journal, 2005,43: 398–412
[47] Denyer K, Clarke B, Hylton C, Tatge H, Smith A M. The elongationof amylose and amylopectin chains in ioslated starch granules. The Plant Journal, 1996, 10(6): 1135–1143
[48] Denyer K, Hylton C M, Jenner C F, Smith A M. Identification of multiple isoforms of soluble and granule–bound starch synthase in developing wheat endosperm. Planta, 1995, 196: 256–265
[49] Denyer K, Johnson P, Zeeman S, Smith A M. The control of amylose synthesis. J.Plant physiol, 2001, 158: 479–487
[50] Denyer K, Sidebottom C, Hylton C H, Smith A M. Soluble isoforms of starch synthase and starch–branching enzyme also occur within starch granules in developing pea embryos. The Plant Journal, 1993, 4: 191–198
[51] Denyer K, Waite D, Edwards A, Martin C, Smith A M. Interaction with amylopectin influences the ability of granule–bound starch synthaseⅠto elongate malto–oligosaccharides. Biochem. J, 1999, 342: 647–653
[52] Dian W, Jiang H, Wu P. Evolution and expression analysis of starch synthase III and IV in rice. J. Exp. Bot. 2005, 56: 623–632
[53] Dinges J R, Colleoni C, Myers A M, James M G. Molecular structure of three mutations at the maize sugary1 locus and their allele–specific phenotypic effects. Plant Physiol, 2001, 125: 1406–1418
[54] Dinges J R, James M G, Myers A M. Mutational analysis of the pullulanase–type debranching enzyme of maize indicates multiple functions in starch metabolism. The Plant Cell, 2003, 15: 666–680
[55] Dinges J R, James M G, Myers A M. Genetic analysis indicates maize pullulanase–and isoamylase–type starch debranching enzymes have partially overlapping functions in starch metabolism. Journal of Applied Glycoscience, 2003, 50: 191–195
[56] Dry I, Smith A M, Edwards E A, Bhattacharyya M, Dunn P, Martin C. Characterisation of cDNAs encoding two isoforms of granule–bound starch synthase which show differential expression in developing storage organs. Plant J, 1992, 2: 193–202
[57] Dynan W S, Jendrisak JJ, Hager D A, Burgess R D. Purification and characterization of wheat germ DNA topoisomeraseⅠ(nicking–closing enzyme). Journal of Biological Chemistry, 1981, 256: 5860–5865
[58] Echt C H and Schwartz D. Evidence for the inclusion of controlling elements within the structural gene at the waxy locus in maize. Genetics, 1981, 99: 275–284
[59] Edwards A, Fulton D C, Hylton C M, Jobling S A, Gidley M, Rossner U, Martin C, Smith A M. A combined reduction in activity of starch synthasesⅡandⅢof potato has novel effects on the starch of tubers. Plant J, 1999, 17: 251–261
[60] Edwards A, Marshall J, Sidebottom C, Visser R G F, Smith A M, Martin C. Biochemical and molecular characterization of a novel starch synthase from potato tubers. The Plant Journal, 1995, 8: 283–294
[61] Emes M J, Bowsher C G, Hedley C, Burrell M M, Scrase–Field E S F, Tetlow I J. Starch synthesis and carbon partitioning in developing endosperm. Journal of Experimental Botany, 2003, 54: 569–575
[62] Fisher D K, Gao M, Kim K N, Boyer C D, Guiltinan M J. Allelic analysis of the maize amylose–extender locus suggests that independent genes encode starch branching enzymes IIa and IIb. Plant Physiol, 1996, 110: 611–619
[63] Flipse E, Suurs L, Keetels C J A, Kossmann J, Jacobsen E, Visser R G F. Introduction of senseand antisense cDNA for branching enzyme in the amylose–free potato mutant leads to physico–chemical changes in the starch. Planta, 1996, 198: 340–347
[64] Francisco P B J, Zhan Y, Park S Y, Ogata N, Yamanouchi H, Nakamura Y. Genomic DNA sequence of a rice gene coding for a pullulanase–type of starch debranching enzyme. Biochem Biophys Acts. 1998, 1387: 469–477
[65] Fujita N, Kubo A, Francisco P B, Nakakita M, Harada K, Minaka N, Nakamura Y. Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice. Planta, 1999, 208: 283-293
[66] Fujita N, Kubo A, Suh D S, Wong K S, Jane J L, Ozawa K, Takaiwa F, Inaba Y, Nakamura Y. Antisense inhibition of isoamylase alters the structure of amylopectin and the physicochemical properties of starch in rice endosperm. Plant Cell Physiol, 2003, 44: 607-618
[67] Fujita N, Yoshida M, Asakura N, Ohdan T, Miyao A., Hirochika H, Nakamura Y. Function and characterization of starch synthase I using mutants in rice. Plant Physiology, 2006, 140: 1070–1084
[68] Funane K, Libessart N, Stewart D, Michishita T, Preiss J. Analysis of essential histidine residues of maize branching enzymes by chemical modification and site–directed mutagenesis. J Protein Chem, 1998, 17(7): 579–90
[69] Gallant D J, Bouchet B, Baldwin P M. Microscopy of starch: evidence of a new level of granule organization. Carbohydrate Polymers, 1997, 32: 177–191
[70] Gao M, Fisher D K, Kim K N, Guiltinan M J. Independent genetic control of maize starch–branching enzymesⅡa andⅡb. Plant Physiology, 1997, 114: 69–78
[71] Gao M, Fisher D K, Kim K N, Shannon J C, Guiltinan M. Evolutionary conservation and expression patterns of maize starch branching enzymeⅠandⅡb genes suggests isoform specialization. Plant Molecular Biology, 1996, 30: 1223–1232
[72] Gerard C, Planchot V, Colonna P, Bertoft E. Relationship between branching density and crystalline structure of A–and B–type maize mutant starches. Carbohydrate Research, 2000, 326: 130–144
[73] Gidley M J and Bulpin P V. Crystallization of malto–oligosaccharides as models of the crystalline forms of starch: minimum chain length requirement for the formation of double helices. Carbohydrate Research, 1987, 161: 291–300
[74] Gir oux M J, Shaw J, Barry G, Cobb B G, Greene T, Okita T, Hannah L C. A single gene mutation that increases maize seed weight. Proc Natl Acad Sci USA, 1996, 93: 5824–5829
[75] Gomez–Casati D F, Lglesias A A. ADP–glucose pyrophosphorylase from wheat endosperm. Purification and characterization of an enzyme with novel regulatory properties. Planta, 2002, 214: 428–434
[76] Guan H P. and Preiss J. Differentiation of the properties of the branching isozymes from maize (Zea mays). Plant Physiol, 1993, 102: 1269–1273
[77] Hager D A and Burgess R R. Elution of proteins from SDS–polyacrylamide gels, removal of SDS, and renaturation of enzymatic activity: results with sigma subunit of E.coli RNApolymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem, 1980, 109: 76–86
[78] Hannah L C and James M. The complexities of starch biosynthesis in cereal endosperms. Current Opinion in Biotechnology, 2008,19: 1–6
[79] Han X Z, Hamaker B R. Amylopectin fine structure and rice starch paste breakdown. Journal of Cereal Science, 2001, 34: 279–284
[80] Harn C, Knight M, Ramakrishnan A, Guan H, Keeling P, Wasserman B P. Isolation and characterization of the zSSⅡa and zSSⅡb starch synthase cDNA clones from maize endosperm. Plant Molecular Biology, 1998, 37: 639–649
[81] Hendriks J H M, Kolbe A, Gibon Y, Stitt M, Geigenberger P. ADP–glucose pyrophosphorylase is activated by post–translational redox–modification in response to light and to sugars in leaves of Arabidopsis and other plant species. Plant Physiology, 2003, 133: 838–849
[82] Hennen–Bierwagen T A, Liu F, Marsh R S, Kim S, Gan Q, Tetlow I J, Emes M J, James M G, Myers A M. Starch biosynthetic enzymes from developing maize endosperm associate in multisubunit complexes. Plant physiol, 2008, 146: 1892–1908
[83] Hizukuri S. Polymodal distribution of the chain lengths of amylopectin, and its significance. Carbohydrate Research, 1986, 147: 342–347
[84] Hizukuri S, Kaneko T, Takeda Y. Measurement of the chain length of amylopectin and its relevance to the origin or crystalline polymorphism of starch granules. Biochemica et Biophysica Acta, 1983,760:188–191
[85] Hung P V, Maeda T, Morita N. Waxy and high–amylose wheat starchs and flours–characteristics, functionality and application. Trends in Food Science & Technology, 2006,17: 448–456
[86] Hussain H., Mant A., Seale R., Zeeman S., Hinchliffe E., Edwards A., Hylton C., Bornemann S., Smith A M., Martin C., and Bustos R. Three forms of isoamylase contribute catalytic properties for the debranching of potato glucans. Plant cell, 2003, 15: 133–149
[87] Imparl–Radosevich JM, Gameon JR, McKean A, Wetterberg D, Keeling P, Guan H. Understanding catalytic properties and functions of maize starch synthase isozymes. Journal of Applied Glycoscience, 2003, 50: 177–182
[88] Ito H, Hamada S, Isono N, Yoshizaki T, Ueno H, Yoshimoto Y, Takeda Y, Matsui H. Functional characteristics of C–terminal regions of starch–branching enzymes from developing seeds of kidney bean (Phaseolus vulgaris L.). Plant Science, 2004, 166 (5): 1149–1158
[89] James M G, Denyer K, Myers A M. Starch synthesis in the cereal endosperm. Current Opinion in Plant Biology, 2003, 6: 215–222
[90] James M G, Robertson D S, Myers A M. Characterization of the maize gene sugary1, a determinant of starch composition in kernels. The plant cell, 1995, 7: 417–429
[91] Jane J L, Ao Z, Duvick S A, Wiklund M, Yoo S H, Wong K S, Gardner C. Structures of amylopectin and starch granules: how are they synthesized. Journal of Applied Glycoscience, 2003, 50 (2): 167–172
[92] Jane J L. Current understanding on starch granule structures. J.Appl. Glycosci, 2006, 53: 205–213
[93] Jenkins J P, Donald A M. The influence of amylose on starch granule structure. International Journal of Biological Macromolecules, 1994, 17: 315–321
[94] Jiang H, Dian W, Wu P. Effect of high temperature on fine structure of amylopectin in rice endosperm by reducing the activity of the starch branching enzyme. Phytochemistry, 2003, 63: 53–59
[95] Jobling Steve. Improving starch for food and industrial applications. Current Opinion in Plant Biology, 2004, 7: 210–218
[96] Jobling S A, Westcott R J, Tayal A, Jaffcoat R, Schwall G P. Production of a freeze–thaw–stable potato starch by antisense inhibition of three starch synthase genes. Nat. Biotecnol, 20: 295–299
[97] Jones H D. Wheat transformation: current technology and applications to grain development and composition. J Cereal Sci, 41: 137–147
[98] Kawagoe Y, Kubo A, Satoh H, Takaiwa F, Nakamura Y. Roles of isoamyloase and ADP–glucose pyrophosphorylase in starch granule synthesis in rice endosperm. The Plant Journal, 2005, 42: 164–174
[99] Kawasaki T, Mizuno K, Baba T, Shimada H. Molecular analysis of the gene encoding a rice starch branching enzyme. Mol. Gen. Gene, 1993, 237: 10–16
[100] Kent F M, William J H, Charlene K T, Olin D A. Starch branching enzymes sbe1 and sbe2 from wheat (Triticum aestivum cv. Cheyenne ): molecular characterization, developmental expression, and homoeologue assignment by differential PCR. Plant Molecular Biology Reporter, 2002, 20: 191a–191m
[101] Kim E G, Ryu S I, Bae H A, Huong N T, Lee S B. Biochemical characterization of a glycogen branching enzyme from Streptococcus mutans: enzymatic modification of starch. Food Chemistry, 2008, 3: 1–6
[102] Kim K N, Fisher D K, Gao M, Guiltinan M. Genomic organization and promoter activity of the maize starch branching enzymeⅠgene. Gene, 1998, 216: 233–243
[103] Kim K N, Fisher D K, Gao M, Guiltinan M. Molecular cloning and characterization of the amylose–extender gene encoding starch branching enzymeⅡb in maize. Plant Molecular Biology, 1998, 38: 945–956
[104] Kleczkowski L A, Villand P, Lu¨thi E, Olsen O A, Preiss J. Insensitivity of barley endosperm ADP–glucose pyrophosphorylase to 3–phosphoglycerate and orthophosphate regulation. Plant Physiology, 1993, 101: 179–186
[105] Kok–Jacon G, Ji Q, Vincken J P, Visser R G F. Towards a more versatileα–glucan biosynthesis in plants. J. Plant physiol, 2003, 160: 765–777
[106] Konik–Rose C, Thistleton J, Chanvrier H, Tan I, Halley P, Michael G, Kosar–Hashemi B, Wang H, Larroque O, Ikea J, McMaugh S, Regina A, Rahman S, Moell M, Li Z. Effects of starch synthaseⅡa gene dosage on grain, protein and starch in endosperm of wheat. Theor Appl Genet, 2007, 122: 631–642
[107] Kosar–Hashemi B, Li Z, Larroque O, Regina A, Yamamori M, Morell M K, Rahman S. Multiple effects of the starch synthaseⅡmutation in developing wheat endosperm. Funct Plant Biol, 2007, 34: 431–438
[108] Kossmann, Jens; Lloyd, James. Understanding and influencing starch biochemistry. Critical Reviews in Plant Sciences, 2000, 19 (3): 171–226
[109] Kossmann J, Visser R G F, Muller–Rober B, Willmitzer L and Sonnewald U. Cloning and expression anaylsis of a potato cDNA that encodes branching enzyme: evidence for co–expression of starch biosynthetic genes. Mol Gen. Genet, 1991, 230: 39–44
[110] Kubo A, Fujita N, Harada K, Matsuda T, Satoh H, Nakamura Y. The starch–debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm. Plant Physiology, 1999, 121: 399–409
[111] Kubo A, Rahman S, Utsumi Y, Li Z Y, Mukai Y, Yamamoto M, Ugaki M, Harada K, Satoh H, Konik–Rose C, Morell M, Nakamura Y. Complementation of sugary–1 phenotype in rice endosperm with the wheat isoamylase1 gene in supports a direct role for isoamylase1 amylopectin biosynthesis. Plant Physiology, 2005, 137: 43–56.
[112] Kuipers A G J, Jacobson E, Visser R G E. Formation and deposition of amylose in the potato tube starch granule are affected by the reduction of granule–bound starch synthase gene expression. Plant Cell, 1994, 6: 43–52
[113] Laemmli U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 1970, 227: 680–685
[114] Lai V M F, Shen M C, Yeh A I, Juliano B O, Lii C Y. Molecular and gelatinization properties of rice starches from IR24 and Sinandomeng cultivars. Cereal Chemistry, 2001, 78: 596–602.
[115] Li Z, Chu X, Mouille G, Yan L, Hashemi B K, Hey S, Napier J, Shewry P, Clarke R, Morell M K, Rahman S. The localization and expression of the classⅡstarch synthases of wheat. Plant physiol, 1999, 120: 1147–1155
[116] Li Z, , Mouille G, Kosar–Hashemi B, Rahman S, Clarke B, Gale K R, Appels R, Morell M K. The structure and expression of the wheat starch synthaseⅢgene. Motifs in the expressed gene define the lineage of the starch synthaseⅢgene family. Plant physiol, 2000, 123: 613–624
[117] Li Z, Rahman S, Kosar–Hashemi B, Mouille G, Appels R, Morell M K. Cloning and characterization of a gene encoding wheat starch synthaseⅠ. Theor Appl Genet, 1999, 98: 1208–1216
[118] Li Z, Sun F, Xu S, Chu X, Mukai Y, Yamamoto M, Ali S, Rampling L, Kosar–Hashemi B, Rahman S, Morell M K. The structural organization of the genes encoding classⅡstarch synthase of wheat and barley and the evolution of the genes encoding starch synthases in plants. Funct Integr Genomics, 2003, 3: 76–85
[119] Lloyd J R, Landschutze V, Kossmann J. Simultaneous antisense inhibition of two starch–synthase isoforms in potato tubers leads to accumulation of grossly modified amylopectin. Biochemistry Journal, 1999, 338: 515–521
[120] Maddelein M L, Libessart N, Bellanger F, Delrue B, D’Hulst C, Ball S. Toward an understanding of the biogenesis of the starch granule: determination of granule–bound and soluble starch synthase functions in amylopectin synthesis. Journal of Biological Chemistry, 1994, 269: 25150–25157
[121] Martin C R, Smith A M. Starch biosynthesis. Plant Cell, 1995, 7: 971–985
[122] Mats B, Hakan L, Anders F, Jansson C. The barley starch granule proteome–internalized granule polypeptides of the mature endosperm. Plant Science, 2004, 166 (3): 617–626
[123] Miura H, Sugawara A. Dosage effects of the three Wx genes on amylose synthesis in wheat endosperm. Theor Appl Genet, 1996, 93: 1066–1070
[124] MizunoK, Kawasaki T, Shimada H, Satoh H, Kobayashi E, Okumura S, Arai Y, Baba T. Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. The Journal of Biological Chemistry, 1993, 268: 19084–19091
[125] MizunoK, Kimura K, Arai Y, Kawasaki T, Shimada H, Baba T. Starch branching enzymes from immature rice seeds. J. Biochem, 1992, 11: 643–651
[126] Mizuno K, Kobayashi E, Tachibana M, Kawasaki T, Fujimura T, Funane K, Kobayashi M, Baba T. Characterization of an isoform of rice starch branching enzyme, RBE4, in developing seeds. Plant Cell Physiology, 2001, 42: 349–357
[127] Morell M K, Blennow A, Hashemi B K, Samuel M S. Differential expression and properties of starch branching nzyme isoforms in developing wheat endosperm. Plant Physiol, 1997, 113: 201–208
[128] Morell M K, Kosar–Hashemi B, Cmiel M, Samuel M S, Chandler P, Rahman S, Buleon A, Batey I L, Li Z. Barley sex6 mutants lack starch synthaseⅡa activity and contain a starch with novel properties. The Plant Journal, 2003, 34:173–185
[129] Morell M, Kosar–Hashemi B, Samuel M, Chandler P, Rahman S, Buelon A, Batey I, Li Z. Identification of the molecular basis of mutations at the barley sex6 locus and their novel starch phenotype. The Plant Journal, 2003, 34: 172–184
[130] Morell M K, Rahman S, Abrahams S L, Appels R. The biochemistry and molecular biology of starch synthesis in cereals. Aust. J. Plant Physiol, 1995, 22: 647–660
[131] Morell M K, Regina A, Li Z, Kosar–Hashemi B, Rahman S. Advances in the understanding of starch synthesis in wheat and barley. Journal of Applied Glycoscience, 2003, 50(2): 217–224
[132] Mouille G, Madddelein M L, Libessart N, Talaga P, Decq A, Delrue B, Ball S. Pre–amylopectin processing: a mandatory step for starch biosynthesis in plants. Plant Cell, 1996, 8: 1353–1366
[133] Mu C, Harn C, Ko Y T, Singletary G W, Keeling P L, Wasserman B P. Association of a 76–kDa polypeptide with soluble starch synthase I activity in maize (cv73) endosperm. Plant J, 1994, 6: 151–159
[134] Mu–Forster C, Huang R, Powers J R, Harriman R W, Knight M, Singletary G.W, Keeling P L, Wasserman B P. Physical association of starch biosynthetic enzymes with starch granules of maize endosperm. Plant physiol, 1996, 111: 821–829
[135] Mukerjea R, Yu L, Robyt J F. Starch biosynthesis: mechanism for the elongation of starch chains. Carbohydrate Research, 2002, 337: 1015–1022
[136] Mutisya J, Sun C, Palmqvist S, Baguma Y, Odhiambo B, Jansson C. Transcriptional regulation of the sbeIIb genes in sorghum (Sorghum bicolor) and barley (Hordeum vulgare): Importance of the barley sbeIIb second intron. Journal of Plant Physiology, 2006, 163 (7): 770–780
[137] Myers A M, Morell M K, James M G, Ball S G. Recent progress toward understanding biosynthesis of the amylopectin crystal. Plant Physiology, 2000,122: 989–997
[138] Nagamine T, Yoshida H, Komae K. Varietal differences and chromosome locations of multiple isoforms of starch branching enzyme in wheat endosperm. Phytochemistry, 1997, 46: 23–26
[139] Nair R B, Baga M, Scoles G J, Kartha K K, Chibbar R N. Isolation, characterization and expression analysis of a starch branching enzymeⅡcDAN from wheat. Plant Science, 1997, 122:153–163
[140] Nakamura T, Vrinten P, Hayakawa K, Ikeda J. Characterization of a granule–bound starch synthase isoform found in the pericarp of wheat. Plant Physiology, 1998,118: 451–459
[141] Nakamura Y. Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis. Plant Science, 1996, 121: 1–18
[142] Nakamura Y. Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue. Plant cell physiol, 2002, 43 (7): 718–725
[143] Nakamura Y and Kazuhiro Y. Changes in enzyme activities associated with carbohydrate metabolism during the development of rice endosperm. Plant Science, 1992, 82:15–20
[144] Nakamura Y, Sakurai A, Inaba Y, Kimura K, Iwasawa N, Nagamine T. The fine structure of amylopectin in endosperm from Asian cultivated rice can be largely classified into two classes. Starch, 2002, 54: 117–131
[145] Nakamura Y, Kubo A, Fujita N, Nishi A, Harada K, Satoh H. Roles of starch debranching enzymes and branching enzymes in amylopectin biosynthesis in rice endosperm. In: Larkin PJ(ed) Agricultural biotechnology: laboratory, field and market. Proc 4th Asian–Pacific Conference on Agric biotech, Darwin, Australia, 1998, pages: 385–387.
[146] Nakamura Y, Kubo A, Shimaniune L. Correlation between activities of starch debranching enzymes andα–polyglucan structure in endosperms of sugary–1 mutants of rice. Plant J, 1997, 12: 143–153
[147] Nakamura Y, Takeichi T, Kawaguchi K. Purification of two forms of starch branching enzyme (Q–enzyme) from developing rice endosperm. Physiologia Plantarum, 1992, 84: 329–335
[148] Nakamura Y, Umemoto T, Ogata N, Kuboki K, Yano M, Sasaki T. Starch debranching enzyme (R–enzyme or pullulanase) from developing rice endosperm: purification, cDNA and chromosomal localization of the gene. Planta, 1996, 199: 209–218
[149] Nakamura Y, Umemoto T, Takahata Y, Amano E. Characteristics and roles of key enzymes associated with starch biosynthesis in rice endosperm. Gamma Field Symp, 1992, 31: 25–44
[150] Nakamura Y, Umemoto T, Takahata Y, Komae K, Amano E, Satoh H. Changes in structure of starch and enzyme activities affected by sugary mutations in developing rice endosperm: possible role of starch debranching enzyme (R–enzyme) in amylopectin biosynthesis. Physiologia Plantarum, 1996, 97: 491–498
[151] Nakamura T, Yamamoto T, Hirano H, Hidaka S, Nagamine T. Production of waxy (amylose–free) wheats. Mol Gen Genet, 1995, 248: 253–259
[152] Nakamura Y, Yuki K, Park SY, Ohya T. Carbohydrate metabolism in the developing endosperm of rice grains. Plant Cell Physiol, 1989, 30 (6): 833–839
[153] Nelson O E, Pan D. Starch synthesis in maize endosperm. Annual Review of Plant Physiology and Plant Molecular Biology, 1995, 46: 475–496
[154] Nishi A, Nakamura Y, Tanaka N, Satoh H. Biochemical and genetic effects of amylose–extender mutation in rice endosperm. Plant physiol, 2001, 127: 459–472
[155] Obana,Y, Omoto, D, Kato C, Matsumoto K, Nagai Y, Kavakli I H, Hamada S, Edwards G E, Okita T W, Matsui H, Ito H. Enhanced turnover of transitory starch by expression of up–regulated ADP–glucose pyrophosphorylase in Arabidopsis thaliana. Plant sci, 2006, 170: 1–11
[156] Pan D, Nelson O E. A debranching enzyme deficiency in endosperms of the sugary–1 mutant of maize. Plant Physiol, 1984, 74: 324–328
[157] Peng M, Gao M, Baga M, Hucl P, Chibbar R N. Starch–branching enzymes preferentially associated with A–type starch granules in wheat endosperm. Plant Physiol, 2000, 124: 265–272
[158] Patindol J, Wang Y J. Fine structures of starches from long grain cultivars with different functionality. Cereal Chemistry, 2002, 79(3): 465–469
[159] Rahman S, Bird A, Regina A, Li Z, Ral J P, McMaugh S, Topping D, Morell M. Resistant starch in cereals: exploiting genetic engineering and genetic variation. Journal of Cereal Science, 2007, 46: 251–260
[160] Rahman S, Hashemi B K, Samuel M S, Hill A, Abbott D C, Skerritt J H, Preiss J, Appels R, Morell M K. The major proteins of wheat endosperm starch granules. Aust. J. Plant Physiol, 1995, 22: 793–803
[161] Rahman S, Li Z, Abrahams S L, Abbott D C, Appels R, Morell M K. Characterisation of a gene encoding wheat endosperm starch branching enzyme–Ⅰ. Theor Appl genet, 1999, 98: 156–163
[162] Rahman S, Li Z, Abrahams S L, Mukai Y, Abbott D C, Samuel M S, Morell M K. Appels R. A complex arrangement of genes at a SBEⅠlocus in wheat. Genome, 1997, 40: 465–474
[163] Rahman S, Li Z, Batey I, Cochrane M P, Appels R, Morell M. Genetic alteration of starch functionality in wheat. Journal of Cereal Science, 2000, 31: 91–110
[164] Rahman S, Nakamura Y, Li Z, Clarke B, Fujita N, Mukai Y, Yamamoto M, Regina A, Tan Z, Kawasaki S, Morell M. Genes for isoamylase in plants: characterization of the sugary–type gene from rice and A.tauschii. Genome, 2003, 46: 496–506
[165] Rahman S, Regina A, Li Z, Mukai Y, Yamamoto M, Hashemi B K, Abrahams S, Morell M K. Comparison of starch–branchinng enzyme genes reveals evolutionary relationships among isoforms. Characterization of a gene for starch–branching enzymeⅡa from the wheat D genome donor Aegilops tauschii. Plant physiol, 2001, 125: 1314–1324
[166] Rahman S, Wong K S, Jane J L, Myers A M, James M G. Characterization of SU1 isomylase, a determinant of storage starch structure in maize. Plant Physiology, 1998, 117: 425–435
[167] Ral J P, Colleoni C, Wattebled F, Dauvillee D, Nempont C, Deschamps P, Li,Z Y, Morell M K, Chibbar R, Purton S, Hulst C, Ball, S.G. Circadian clock regulation of starch metabolism establishes GBSSI as a major contributor to amylopectin synthesis in Chlamydomonas reinhardtii. Plant Physiology, 2006, 142 (1): 305–317
[168] Regina A, Bird D, Topping D, Bowden S, Freeman J, Barsby T, Hashemi B K, Li Z, Rahman S, Morell M. High amylose wheat generated by RNA–interference improves indices of large bowel health in rats. Proc. Natl. Acad. Sci. USA, 2006, 103: 3546–3551.
[169] Regina A, Kosar H B, Li Z, Pedler A, Mukai Y, Yamamoto M, Gale K, Sharp P J, Morell M K, Rahman S. Starch branching enzyme IIb in wheat is expressed at low levels in the endosperm compared to other cereals and encoded at a non–syntenic locus. Planta, 2005, 222 (5): 899–909
[170] Regina A, Kosar–Hashemi B, Li Z, Rampling L, Cmiel M, Gianibelli C, Konik–Rose C, Larroque O, Rahman S, Morell M K. Multiple isoforms of starch branching enzyme I in wheat: lack of the major SBE–I isoform does not alter starch phenotype. Funct Plant Biol, 2004, 31: 591–601
[171] Repellin A, Baga M, Chibbar R N. Characterization of a cDNA encoding a type I starch branching enzyme produced in developing wheat (Triticum aestivum L.) kernels. J. Plant Physiol, 2001, 158: 91–100
[172] Roldán I, Wattebled F, Mercedes L M, DelvalléD, Planchot V, Jiménez S, Pérez R, Ball S, D’Hulst C, Mérida A. The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggest a novel function of elongation enzymes in the control of starch granule formation. Plant J, 2007, 49: 492–504
[173] Rydberg U, Andersson L, Andersson R A P, Larsson H. Comparison of starch branching enzyme I and II from potato. European Journal of Biochemistry, 2001, 268: 6140–6145
[174] Safford R, Jobling S, Sidebottom C M, Westcott R J, Cooke D, Tober K J, Strongitharm B H, Russell A L, Gidley M J. Consequences of antisense RNA inhibition of starch branching enzyme activity on properties of potato starch. Carbohydr.Polymers, 1998, 35: 155–168
[175] Sakulsingharoja C, Choi S B, Hwang S K, Edwards G E, Bork J, Meyer C R, Preiss J, Okita T W. Engineering starch biosynthesisfor increasing rice seed weight: the role of the cytoplasmic ADP–glucose pyrophosphorylase. Plant sci, 2004, 167: 1323–1333
[176] Sano Y. Differential regulation of waxy gene expression in rice endosperm. Theoretical and Applied Genetics, 1984, 68: 467–473
[177] Satoh H, Nishi A, Yamashita K, Takemoto Y, Tanaka Y, Hosaka Y, Sakurai A, Fujita N, Nakamura Y. Starch–branching enzyme I–deficient mutation specifically affects the structure and properties of starch in rice endosperm. Plant Physiol, 2003, 133: 1111–1121
[178] Scafford R, Jobling S A, Sidebottom C M, Westcott R J, Cooke D, Tober K J, Strongitharm B H, Russell A L, Gidley M J. Consequences of antisense RNA inhibition of starch branching enzyme activity on properties of potato starch. Carbohydr. Polym, 35:155–168
[179] Schultz J A and Juvik J A. Current models for starch synthesis and the sugary enhancer1(se1) mutation in zea mays. Plant Physiology and Biochemistry, 2004, 42: 457–464
[180] Schwall G P, Safford R, Westcott R J, Jeffcoat R J, Tayal A, Shi Y C, Gidley M G, Jobling S A. Production of very–high–amylose potato starch by inhibition of SBE A and SBE B. Nation Biotechnology, 2000, 18: 551–554
[181] Sehnke PC, Chung H J, Wu K, Ferl RJ. Regulation of starch accumulation by granule–associated plant 14–3–3 proteins. Proceedings of the National Academy of Sciences USA, 2001, 98: 765–770
[182] Seo B S, Kim S, Scott M P, Singletary G W, Wong K S, James M G, Myers A M. Functional interactions between heterologously expressed starch–branching enzymes of maize and glycogen synthases of brewer’s yeast. Plant Physiol, 2002, 128: 1189–1199
[183] Shibanuma K, Takeda Y, Hizukuri S, Shibata S. Molecular structures of some wheat starches. Carbohydrate Polymers, 1994, 25, 111–116
[184] Shimada T, Otani M, Hamada T, Kim S H. Increase of amylose content of sweetpotato starch by RNA interference of the starch branching enzymeⅡgene (Ⅰb SBEⅡ). Plant Biotechnology, 2006, 23: 85–90
[185] Sidebottom C, Kirkland M, Strongitharm B, Jeffcoat R. Characterization of the difference of starch branching enzyme activities in normal and low–amylopectin maize during kernel development. Journal of Cereal Science, 1998, 27: 279–287
[186] Sikka VK, Choi S, Kavakli I H, Sakulsingharoj C, Gupta S, Ito H, Okita TW. Subcellular compartmentation and allosteric regulation of the rice endosperm ADPglucose pyrophosphorylase. Plant Science, 2001, 161: 461–468
[187] Skerritt J H, Frend A J, Robson L G, and Greenwell P. Immunological homologies between wheat gluten and starch granules protein. Journal of Cereal Science, 1990, 12: 123–136
[188] Skylas D J, Dyk D V, Wrigley C W. Proteomics of wheat grain. Journal of Cereal Science, 2005, 41: 165–179
[189] Slattery C J, Kavakli I H, Okita T W. Engineering strach for increased quantity and quality. Trends in Plant Science, 2000, 5: 291–298
[190] Smith A M. The biosynthesis of starch granules. Biomacromolecules, 2001, 2: 335–341
[191] Smith A M, Denyer K, Martin C R. What controls the amount and structure of starch in storage organs. Plant Physiol, 1995, 107: 673–677
[192] Smith A M, Denyer K, Martin C R. The synthesis of the starch granule. Annu. Rev. Plant Physiol. Plant Mol. Biol, 1997, 48: 67–87
[193] Song Y, Jane J. Characterization of barley starches of waxy, normal, and high amylose varieties. Carbohydrate Polymers, 2000, 41: 365–377
[194] Stark D M, Timmerman K P, Barry G F, Preiss J, Kishore G M. Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science, 1992, 258: 287–292
[195] Sun C, Sathish P, Ahlandsberg S, Deiber A, Jansson C. Identification of four starch–branching enzymes in barley endosperm: partial purification of forms I, IIa and IIb. New Phytology, 1997, 137: 215–222
[196] Sun C, Sathish P, Ahlandsberg S, Jansson C. The two genes encoding starch–branching enzymes IIa and IIb are differentially expressed in barley. Plant Physiol, 1998, 118: 37–49
[197] Suzuki G, Moriyama M, Fujioka K, Yamamoto M, Subramanyam N C, Li Z, Appels R, Morell M, Mukai Y, Rahman S. The starch branching enzymeⅠlocus from Aegilops tauschii, the donorof the D genome to wheat. Functional and integrative genomics, 2003, 3: 69–75
[198] Takaoka M, Watanabe S, Sassa H, Yamamori M, Nakamura T, Sasakuma T, Hirano H. Structural characterization of high molecular weight starch granule–bound proteins in wheat (Triticum aestivum L.). J. Agric. Food Chem, 1997, 45: 2929–2934
[199] Takashi K, Guan H, Sivak M, Preiss J. Analysis of the active center of branching enzyme II from maize endosperm. Journal of Protein Chemistry, 1996, 15(3): 305–313
[200] Takeda Y, Guan H P, Preiss J. Branching of amylose by the branching isoenzymes of maize endosperm. Carbohydr Res, 1993, 240: 253–263
[201] Tanaka N, Fujita n, Nishi A, Satoh H, Hosaka Y, Ugaki M, Kawasaki S, Nakamura Y. The structure of strach can manipulated by changing the expression levels of starch branching enzymeⅡb in rice endosperm. Plant Biotechnology Journal, 2004, 2: 507–516
[202] Tatge H, Marshall J, Martin C, Edwards E A, Smith A M. Evidence that amylose synthesis occurs within the matrix of the starch granule in potato tubers. Plant Cell and Environment, 1999, 22 (5): 543–550
[203] Tetlow I J. Starch synthesis and carbohydrate oxidation in amyloplastes from developing wheat endosperm. Planta, 1994, 194:454–460
[204] Tetlow I J. Understanding storage starch biosynthesis in plants: a means to quality improvement. Can. J. Bot, 2006, 84: 1167–1185
[205] Tetlow I J, Avies E J, Vardy K A, Bowsher C G, Burrell M M, Emes M J. Subcellular localization of ADP–glucose pyrophosphorylase in developing wheat endosperm and analysis of a plastidial isoform. J. Exp. Bot, 2003, 54: 715–725
[206] Tetlow I J, Beisel K G, Cameron S, Makhmoudova A, Liu F, Bresolin N S, Wait R, Morell M K, Emes M J. Analysis of protein complexes in wheat amyloplasts reveals functional interactions among starch biosynthetic enzymes. Plant physiol, 2008, 146: 1878–1891
[207] Tetlow I J, Morell M K, Emes M J. Recent developments in understanding the regulation of starch metabolism in higher plants. Journal of Experimental Botany, 2004, 55: 2131–2145
[208] Tetlow I J, Wait R, Lu Z X, Akkasaeng R, Bowsher C G, Esposito S, Hashemi B K, Morell M K, Emes M J. Protein phosphorylation in amyloplasts regulates starch branching enzyme activity and protein–protein interactions. Plant Cell, 2004, 16: 694–708
[209] Thompson DB. On the non–random nature of amylopectin branching. Carbohydrate Polymers, 2000, 43: 223–239
[210] Tiessen A, Hendriks J H M, Stitt M, Branscheid A, Gibon Y, FarréE M, Geigenberger P. Starch synthesis in potato tuber is regulated by post–translational redox modification of ADP–glucose pyrophosphorylase. The Plant Cell, 2002, 14: 2191–2213
[211] Tiessen A, Prescha K, Branscheid A, Palacios N, McKibbin R, Halford N G, Geigenberger P. Evidence that SNF1–related kinase and hexokinase are involved in separate sugar–signalling pathways modulating post–translational redox activation of ADPglucose pyrophosphorylase in potato tubers. The Plant Journal, 2003, 35: 490–500
[212] Tomlinson K, Lloyd J R, Smith A M. Importance of isoforms of starch–branching enzyme in determing the structure of starch in pea leaves. Plant J, 1997, 11: 31-43
[213] Tsai C Y, Salamini F, Nelson O E. Enzymes of carbohydrate metabolism in the developing endosperm of maize. Plant physiol, 1970, 46: 299–306
[214] Umemoto T, Aoki N, Lin H X, Nakamura Y, Inouchi N, Sato Y I, Yano M, Hirabayashi H, Maruyama S. Natural variation in rice starch synthaseⅡa affects enzyme and starch properties. Funct Plant Biol, 2004, 31: 671–684
[215] Umemoto T and Aoki N. Single–nucleotide polymorphisms in rice starch synthaseⅡa that alter starch gelatinization and starch associationof the enzyme. Funct Plant Biol, 2005, 32: 763–768
[216] Umemoto T, Yano M, Satoh H, Shomura A, Nakamura Y. Mapping of a gene responsible for the difference in amylopectin structure between japonica–type and indica–type rice varieties. Theor Appl Genet, 2002, 104: 1–8
[217] Utsumi Y and Nakamura Y. Structural and enzymatic characterization of the isoamylase1 homo–oligomer and the isoamylase1–isoamylase2 hetero–oligomer from rice endosperm. Planta, 2006, 225: 75–87
[218] Vandeputte G E, Delcour J A. From sucrose to starch granule to starch physical behaviour: a focus on rice starch. Carbohydrate Polymers, 2004, 58: 245–266
[219] Van de Wal M, D’Hulst C, Vincken J–P, Buleon A, Visser R, Ball S. Amylose is synthesized in vitro by extension of and cleavage from amylopectin. The Journal of Biological Chemistry, 1998, 273: 22232–22240
[220] Vasil I K. Molecular genetic improvement of cereals: transgenic wheat (Triticum aestivum L.). Plant Cell Rep, 2007, 26: 1133–1154
[221] Vermeylen R, Goderis B, Reynaers H, Delcour J A. Amylopectin molecular structure reflected in macromolecular organization of granular starch. Biomacromolecules, 2004, 5: 1775–1786
[222] Villand P, Kleczowski L. Is there an alternative pathway for starch biosynthesis in cereal seeds. Z. Natuirforsch. Teil C, 1994, 49: 215–219
[223] Visser R G F, Somhorst I, Kuipers G J, Ruys N J, Feenstra W J, Jacobsen E. Inhibition of the expression of the gene for granule–bound starch synthase in potato by antisense constructs. Mol. Gen. Genet, 1991, 225: 289–296
[224] Vos–Scheperkeuter G H, Boer W. de, Visser R F G, Feenstra W J, Witholt B. Identification of granule–bound starch synthase in potato tubers. Plant Physiol, 1986, 82: 411–416
[225] Vrinten P and Nakamura T. Wheat granule–bound starch synthaseⅠandⅡare encoded by separate genes that are expressed in different tissues. Plant Physiol, 2000, 122: 253–263
[226] Wang T L, Bogracheva T Y, Hedley C L. Starch: as simple as A, B, C. Journal of Experimental Botany, 1998, 49: 481–502
[227] Wang Z, Chen X, Wang J, Liu Y, Zhao L, Wang G. Increasing maize seed weight by enhancing the cytoplasmic ADP–glucose pyrophosphorylase activity in transgenic plants.Plant Cell Tiss Organ Cult, 2007, 88: 83–92
[228] Wattebled F, Dong Y, Dumez S, Delvalle D, Planchot V, Berbezy P, Vyas D, Colonna P, Chatterjee M, Ball S, D’Hulst C. Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate phytoglycogen and an abnormal form of amylopectin. Plant Physiol, 2005, 138: 184–195
[229] Wasserman BP, Harn C, Mu–Forster, C, Huang R. Progress towards genetically modified starches. Cereal Foods World, 1995, 40 (11): 810–817
[230] Wong K S, Kubo A, Jane J L, Harada K, Satoh H, Nakamura Y. Structures and properties of amylopectin and phytoglycogen in the endosperm of sugary–1 mutants of rice. Journal of Cereal Science, 2003, 37: 139–149
[231] Wu C, Colleoni C, Myers A M, James M G. Enzymatic properties of ZPU1, the maiz pullulanase–type starch debranching enzyme. Arch. Bioche.Biophys, 2002, 406: 21–32
[232] Yamanouchi H, Nakamura Y. Organ specificity of isoforms of starch branching enzyme (Q–enzyme) in rice. Plant Cell Physiol, 1992, 33: 985–991
[233] Yamamori M, Endo T R. Variation of starch granule proteins and chromosome mapping of their coding genes in common wheat. Theor Appl genet, 1996, 93: 275–281
[234] Yamamori M, Fujita S, Hayakawa K, Matsuki J, Yasui T. Genetic elimination of a starch granule protein, SGP–1, of wheat generates an altered starch with apparent high amylose. Theor Appl genet, 2000, 101: 21–29
[235] Yamamori Y, Nakamura T, Kuroda A, Variations in the content of starch granule–bound protein among several Japanese cultivars of common wheat (Triticum aestivum L.). Euphytica, 1992, 64:215–219
[236] Yao Y, Thompson D B, Guiltinan M J. Maize starch–branching enzyme isoforms and amylopectin structure. In the absence of starch–branching enzymeⅡb, the further absence of starch–branching enzymeⅠa leads to increased branching. Plant Physiol, 2004, 136: 3515–3523
[237] Yu Y, Mu H H, Mu–Forster C, Wasserman B P. Polypeptides of the maize amyloplast stroma. Plant Physiol, 1998, 116: 1451–1460
[238] Zeeman S C, Northrop F, Smith A M, Rees T. A starch–accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch–hydrolysing enzyme. The Plant Journal, 1998, 15: 357–365
[239] Zeeman S C, Smith S M, Smith A M. The priming of amylose synthesis in Arabidopsis leaves. Plant physiology, 2002, 128: 1069–1076
[240] Zeeman S C, Tiessen A, Pilling E, Kato L, Donald A M, Smith A M. Starch synthesis in Arabidopsis: granule synthesis, composition, and structure. Plant Physiology, 2002, 129: 516– 529
[241] Zeeman S C, Umemoto T, Lue W L, Au–Yeung P, Martin C, Smith A M, Chen J. A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell, 1998, 10:1699–1712
[242] Zhang X, Colleoni C, Ratushna V, Sirghie C M, James M G, Myers A M. Molecular characterization demonstrates that the Zea mays gene sugary–2 codes for the starch synthase isoform SSⅡa. Plant Mol Biol, 2004, 54: 865–879
[243] Zhang X, Myers A M, James M G. Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis. Plant Physiol, 2005, 138: 663–674
[244] Zhao X C, Batey I L, Sharp P J, Crosbie G, Barclay I, Wilson R, Morell M K, Appels R. A single genetic locus associates with starch granule properties and noodle quality in wheat. J Cereal Sci, 1998, 27: 7–13
[245] Zhu Z P, Hylton C M, Roessner U, Smith A M. Characterization of starch debranching enzyme in pea embryos. Plant Physiology, 1998, 118: 581–590