Identification and characterization of a thermostable GH11 xylanase from Paenibacillus campinasensis NTU-11 and the distinct roles of its carbohydrate-binding domain and linker sequence.

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作者： Lijuan,Wang ^[1] ; Yiya,Wang ^[1] ; Siyuan,Chang ^[2] ; Zhen,Gao ^[3] ; Jiangfeng,Ma ^[4] ; Bin,Wu ^[1] ; Bingfang,He ^[5] ; Ping,Wei ^[1]

作者单位： College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, 30 Puzhunan Road, Nanjing 211810, Jiangsu, China. ^[1] School of Health and Life Science, Nanjing Polytechnic Institute, 625 Geguan Road, Nanjing 210048, Jiangsu, China. ^[2] College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, 30 Puzhunan Road, Nanjing 211810, Jiangsu, China. Electronic address: gaozhen_njtech@163.com. ^[3] College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, 30 Puzhunan Road, Nanjing 211810, Jiangsu, China. Electronic address: majiangfeng@njtech.edu.cn. ^[4] School of Pharmaceutical Sciences, Nanjing Tech University, 30 Puzhunan Road, Nanjing 211816, Jiangsu, China. ^[5]

关键词 Carbohydrate-binding module Paenibacillus campinasensis Thermal-stability Xylanase

主题词酶稳定性(Enzyme Stability);大肠杆菌(Escherichia coli);氢离子浓度(Hydrogen-Ion Concentration);类芽孢杆菌属(Paenibacillus);重组蛋白质类(Recombinant Proteins);底物特异性(Substrate Specificity);木聚糖类(Xylans)

DOI 10.1016/j.colsurfb.2021.112167

PMID 34715594

发布时间 2021-12-14

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