Characterization of a fungal thermostable endoglucanase from Chinese Nong-flavor daqu by metatranscriptomic method

被引:22
作者
Ali, Barkat [1 ,2 ,3 ]
Yi, Zhuolin [1 ,2 ]
Fang, Yang [1 ,2 ]
Chen, Lanchai [1 ,2 ,3 ,4 ]
He, Maize [1 ,2 ]
Liu, Dayu [5 ]
Luo, Huibo [6 ]
Zhao, Dong [7 ]
Zheng, Jia [7 ]
He, Hui [8 ]
Jin, Yanling [1 ,2 ]
Zhao, Hai [1 ,2 ]
机构
[1] Chinese Acad Sci, Key Lab Environm & Appl Microbiol, Chengdu 610041, Sichuan, Peoples R China
[2] Chinese Acad Sci, Chengdu Inst Biol, Environm Microbiol Key Lab Sichuan Prov, Chengdu 610041, Sichuan, Peoples R China
[3] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[4] Sichuan Univ, Coll Life Sci, Key Lab Bioresources & Ecoenvironm, Minist Educ, Chengdu 610065, Sichuan, Peoples R China
[5] Chengdu Univ, Coll Pharm & Biol Engn, Meat Proc Applicat Key Lab Sichuan Prov, Chengdu 610106, Sichuan, Peoples R China
[6] Sichuan Univ Sci & Engn, Bioengn Coll, Liquor Making Biotechnol Applicat Key Lab Sichuan, Zigong 64300, Peoples R China
[7] Wuliangye Grp, Yibin 644007, Peoples R China
[8] Moutai Coll, Dept Liquor Making Engn, Renhuai 564501, Peoples R China
关键词
Chinese Nong-flavor daqu; Fungal endo-beta-glucanase; beta-Glucan degradation; Metatranscriptomics-based method; BIOCHEMICAL-CHARACTERIZATION; BETA-1,3-1,4-GLUCANASE LICHENASE; PURIFICATION; EXPRESSION; OVEREXPRESSION; FERMENTATION; DIVERSITY; GENE;
D O I
10.1016/j.ijbiomac.2018.09.173
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chinese Nong-flavor (NF) daqu has been enriched with plenty of active enzymes by man-made environment for thousand years. Based on our previous metatranscriptomics, an endo-beta-glucanase gene (NFEg16A), which showed high expression level in NF daqu, was directly obtained and expressed in Escherichia coli BL21 (DE3). NFEg16A shared the highest sequence identity of 87% with endo-1,3-1,4-beta-glucanase from Paecilomyces thermophile. It was optimally active at pH 6.5 and 60 degrees C and highly stable (>75% residual activity) at pH 3-8 and temperature 30-90 degrees C. The activity of NFEg16A was strongly inhibited by 10 mM Fe3+ and Hg2+. Compared with endoglucanases with high similarities, NFEg16A was more stable at 70 degrees C and had higher half-lives of 3.4 h and 1.4 hat 80 degrees C and 90 degrees C, respectively. Its specific activity was 85.3 U/mg on barley beta-glucan. Moreover, NFEg16A could efficiently hydrolyze substrate at high concentration of 15 mg/mL, and released glucose and cellobiose as its main end-products. Therefore, this work to some extent verified the important role of NFEg16A in NF daqu, and it would stimulate the acquisition of more enzymes from NF daqu to improve the baijiu quality in future. High thermostability of NFEg16A could also strengthen its potential applications in feed industry. (C) 2018 Published by Elsevier B.V.
引用
收藏
页码:183 / 190
页数:8
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