Improved thermostability of a metagenomic glucose-tolerant β-glycosidase based on its X-ray crystal structure
作者: Tomohiko MatsuzawaMasahiro WatanabeKatsuro Yaoi
作者单位: 1National Institute of Advanced Industrial Science and Technology (AIST)
刊名: Applied Microbiology and Biotechnology, 2017, Vol.101 (23-24), pp.8353-8363
来源数据库: Springer Journal
DOI: 10.1007/s00253-017-8525-9
关键词: Β-glycosidaseMetagenomeBiomassThermostabilization
英文摘要: MeBglD2, a metagenomic β-glycosidase, is stimulated by various saccharides, including d -glucose, d -xylose, and maltose, and it promotes the enzymatic saccharification of plant biomass. To improve the thermostability of MeBglD2, its X-ray crystal structure was analyzed, and the amino acid residues responsible for its thermostability were identified using the structural information. Mutations in His8, Asn59, and Gly295 improved the thermostability of MeBglD2, and the combination of these mutations resulted in the highest thermostability. Compared with wild-type MeBglD2, thermostable MeBglD2 mutants promoted plant biomass saccharification using Trichoderma reesei cellulase. In addition to thermostability, the thermostable mutants exhibited higher tolerance to ethanol, dimethyl sulfoxide,...
原始语种摘要: MeBglD2, a metagenomic β-glycosidase, is stimulated by various saccharides, including d -glucose, d -xylose, and maltose, and it promotes the enzymatic saccharification of plant biomass. To improve the thermostability of MeBglD2, its X-ray crystal structure was analyzed, and the amino acid residues responsible for its thermostability were identified using the structural information. Mutations in His8, Asn59, and Gly295 improved the thermostability of MeBglD2, and the combination of these mutations resulted in the highest thermostability. Compared with wild-type MeBglD2, thermostable MeBglD2 mutants promoted plant biomass saccharification using Trichoderma reesei cellulase. In addition to thermostability, the thermostable mutants exhibited higher tolerance to ethanol, dimethyl sulfoxide,...
全文获取路径: Springer  (合作)
分享到:
来源刊物:
影响因子:3.689 (2012)

×
关键词翻译
关键词翻译
  • thermostable 耐热的
  • crystal 晶体
  • glycosidase 糖苷酶
  • improved 改进
  • cellulase 纤维酶
  • glucose 葡萄糖
  • structure 构造
  • addition 添加
  • sulfoxide 亚砜
  • enzymatic 酶催的