Isolation and characterization of a non-specific endoglucanase from a metagenomic library of goat rumen

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• 作者：Jianbo Cheng ; Shuai Huang ; Haiqin Jiang…
• 关键词：Endoglucanase ; Xylanase ; Metagenome ; Goat rumen
• 刊名：World Journal of Microbiology & Biotechnology
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：32
• 期：1
• 全文大小：967 KB
• 参考文献：An N, Li LM, Xu FZ, Cheng JB (2010) Construction and analysis of rumen bacterial artificial chromosome library from a goat rumen micronora. ACTA Laser Biol Sinica 19:659–662
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• 作者单位：Jianbo Cheng (1)
  Shuai Huang (1)
  Haiqin Jiang (1)
  Yunhai Zhang (1) (2)
  Lvmu Li (1)
  Juhua Wang (1)
  Caiyun Fan (1) (2)
  
  1. College of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People’s Republic of China
  2. Anhui Provincial Laboratory for Local Livestock & Poultry Genetic Resource Conservation and Bio-Breeding, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People’s Republic of China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Applied Microbiology
  Biotechnology
  Biochemistry
  Environmental Biotechnology
  Microbiology
  
• 出版者：Springer Netherlands
• ISSN：1573-0972

文摘

A cellulase gene (cel28a) was isolated from a rumen microbial metagenome library of goat rumen microorganisms, cloned into E. coli, and expressed in active form. The gene has a length of 1596 bp obtained using a genome walking Kit and encodes a protein of 509 amino acids with a calculated MW of 55 kDa. The deduced amino acid sequence was homologous with cellulases belonging to the glycosyl hydrolase family 5 (GH5). The expressed protein showed activity toward carboxymethylcellulose (CMC) and xylan, suggesting non-specific endoglucanase activity. The optimal conditions for endoglucanase and xylanase activities were 50 °C and pH 5.0. The metal ions (Ca2+, Fe2+, Mn2+ and Co2+) stimulated the cellulase activity of cel28a, while the other metal ions and chemicals (Ni2+, Mg2+, Zn2+, Cu2+, SDS and EDTA) inhibited the cellulase activity. Further examination of substrate preference showed a higher activity with CMC, oat spelt xylan and birchwood xylan than with filter paper and microcrystalline cellulose, again suggesting that the protein was an endoglucanase with xylanase activity.