A thermo-halo-tolerant and proteinase-resistant endoxylanase from Bacillus sp. HJ14

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• 作者：Junpei Zhou (1) (2) (3)
  Qian Wu (1) (2) (3)
  Rui Zhang (1) (2) (3)
  Minghe Mo (4)
  Xianghua Tang (1) (2) (3)
  Junjun Li (1) (2) (3)
  Bo Xu (1) (2) (3)
  Junmei Ding (1) (2) (3)
  Qian Lu (2)
  Zunxi Huang (1) (2) (3)
  
• 刊名：Folia Microbiologica
• 出版年：2014
• 出版时间：September 2014
• 年：2014
• 卷：59
• 期：5
• 页码：423-431
• 全文大小：2,360 KB
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• 作者单位：Junpei Zhou (1) (2) (3)
  Qian Wu (1) (2) (3)
  Rui Zhang (1) (2) (3)
  Minghe Mo (4)
  Xianghua Tang (1) (2) (3)
  Junjun Li (1) (2) (3)
  Bo Xu (1) (2) (3)
  Junmei Ding (1) (2) (3)
  Qian Lu (2)
  Zunxi Huang (1) (2) (3)
  
  1. Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People’s Republic of China
  2. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People’s Republic of China
  3. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People’s Republic of China
  4. Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, 650091, People’s Republic of China
  
• ISSN：1874-9356

文摘

A glycosyl hydrolase family 10 endoxylanase from Bacillus sp. HJ14 was grouped in a separated cluster with another six Bacillus endoxylanases which have not been characterized. These Bacillus endoxylanases showed less than 52?% amino acid sequence identity with other endoxylanases and far distance with endoxylanases from most microorganisms. Signal peptide was not detected in the endoxylanase. The endoxylanase was expressed in Escherichia coli BL21 (DE3), and the purified recombinant enzyme (rXynAHJ14) was characterized. rXynAHJ14 was apparent optimal at 62.5?°C and pH 6.5 and retained more than 55?% of the maximum activity when assayed at 40-5?°C, 23?% at 20?°C, 16?% at 85?°C, and even 8?% at 0?°C. Half-lives of the enzyme were more than 60?min, approximately 25 and 4?min at 70, 75, and 80?°C, respectively. The enzyme exhibited more than 62?% xylanase activity and stability at the concentration of 3-0?% (w/v) NaCl. No xylanase activity was lost after incubation of the purified rXynAHJ14 with trypsin and proteinase K at 37?°C for 60?min. Different components of oligosaccharides were detected in the time-course hydrolysis of beechwood xylan by the enzyme. During the simulated intestinal digestion phase in vitro, 11.5-9.0, 15.3-9.0, 21.9-7.7, and 28.2-1.2?μmol/mL reducing sugar were released by the purified rXynAHJ14 from soybean meal, wheat bran, beechwood xylan, and rapeseed meal, respectively. The endoxylanase might be an alternative for potential applications in the processing of sea food and saline food and in aquaculture as agastric fish feed additive.