A novel thermophilic endo-β-1,4-mannanase from Aspergillus nidulans XZ3: functional roles of carbohydrate-binding module and Thr/Ser-rich linker region

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• 作者：Haiqiang Lu (1)
  Huiying Luo (1)
  Pengjun Shi (1)
  Huoqing Huang (1)
  Kun Meng (1)
  Peilong Yang (1)
  Bin Yao (1)
  
• 关键词：β ; Mannanase ; Thermophilic ; CBM ; Linker region ; Thermostability
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2014
• 出版时间：March 2014
• 年：2014
• 卷：98
• 期：5
• 页码：2155-2163
• 全文大小：388 KB
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• 作者单位：Haiqiang Lu (1)
  Huiying Luo (1)
  Pengjun Shi (1)
  Huoqing Huang (1)
  Kun Meng (1)
  Peilong Yang (1)
  Bin Yao (1)
  
  1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing, 100081, People’s Republic of China
  
• ISSN：1432-0614

文摘

The gene man5XZ3 from Aspergillus nidulans XZ3 encodes a multimodular β-mannanase of glycoside hydrolase family 5 that consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain. Recombinant Man5XZ3 and its two truncated derivatives, Man5ΔCBM (removing the CBM1) and Man5ΔCL (removing both the CBM1 and linker region), were produced in Pichia pastoris and showed significant variance in the secondary structure. The three enzymes had similar biochemical properties, such as optimal pH and temperature (pH?5.0 and 80?°C) and excellent pH stability at pH?4.0-0.0. Removal of the CBM1 alone could improve the thermostability of Man5XZ3, but further removal of the linker region resulted in worse thermostability. Man5XZ3 retained greater enzyme activity in the presence of an organic solvent (acetone), two detergents (SDS and Triton X-100), and a chaotropic agent (urea) compared with Man5ΔCBM and Man5ΔCL. This study provides an excellent β-mannanase candidate favorable for various industries and primarily demonstrates the relationship between enzyme structure and function.