A Fungal Alpha-Galactosidase from Pseudobalsamia microspora Capable of Degrading Raffinose Family Oligosaccharides

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• 作者：Dongxue Yang ; Guoting Tian ; Fang Du…
• 关键词：Pseudobalsamia microspora ; Purification and characterization ; Alpha ; galactosidase ; Chemical modification ; Degradation
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2015
• 出版时间：August 2015
• 年：2015
• 卷：176
• 期：8
• 页码：2157-2169
• 全文大小：588 KB
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• 作者单位：Dongxue Yang (1)
  Guoting Tian (2)
  Fang Du (1)
  Yongchang Zhao (2)
  Liyan Zhao (3)
  Hexiang Wang (1)
  Tzi Bun Ng (4)
  
  1. State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, 100193, People’s Republic of China
  2. Institute of Biotechnology and Germplasmic Resource, Yunnan Academy of Agricultural Science, Kunming, 650223, People’s Republic of China
  3. College of Food Science and Technology, Nanjing Agricultural University, Weigang, Nanjing, 210095, People’s Republic of China
  4. School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, People’s Republic of China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Biochemistry
  
• 出版者：Humana Press Inc.
• ISSN：1559-0291

文摘

An alpha-galactosidase was purified from Pseudobalsamia microspora (PMG) to 1224.1-fold with a specific activity of 11,274.5units/mg by ion-exchange chromatography and gel filtration. PMG is a monomeric protein with a molecular mass of 62kDa as determined by SDS-PAGE and by gel filtration. Chemical modification using N-bromosuccinimide (NBS) resulted in a complete abrogation of the activity of PMG, suggesting that Trp is an amino acid essential to its activity. The activity was strongly inhibited by Hg2+, Cd2+, Cu2+, and Fe3+ ions. Three inner peptide sequences for PMG were obtained by liquid chromatography–tandem mass spectrometry (LC–MS–MS) analysis. When 4-nitrophenyl α-d-glucopyranoside (pNPGal) was used as substrate, the optimum pH and temperature of PMG were 5.0 and 55°C, respectively. The Michaelis constant (K m) value of the alpha-galactosidase on pNPGal was 0.29mM, and the maximal velocity (V max) was 0.97μmolmln∮ Investigation by thin-layer chromatography (TLC) demonstrated its ability to hydrolyze raffinose and stachyose. Hence, it can be exploited in degradation of non-digestible oligosaccharides from food and feed industries.