研究报告

白酒酒糟中产纤维素酶细菌的分离筛选和酶学性质研究

  • 宋丽丽 ,
  • 闻格 ,
  • 霍姗浩 ,
  • 胡晓龙 ,
  • 杨旭 ,
  • 张志平
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  • 1(郑州轻工业大学 食品与生物工程学院,河南 郑州,450001);
    2(河南仰韶酒业有限公司 博士后创新实践基地,河南 三门峡,472000)
博士,讲师(本文通讯作者,E-mail:songlili191@163.com)

收稿日期: 2019-12-17

  网络出版日期: 2020-05-19

基金资助

国家自然科学基金(31801535);河南省重大科技专项项目(181100211400);郑州轻工业大学博士基金(2013BSJJ005)

Screening and identification of a cellulase-producing bacterium from distiller′s grains and the enzymatic property

  • SONG Lili ,
  • WEN Ge ,
  • HUO Shanhao ,
  • HU Xiaolong ,
  • YANG Xu ,
  • ZHANG Zhiping
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  • 1(School of Food and Bio-engineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China);
    2(Postdoctoral Research & Development Base, Yangshao Distillery Co. Ltd., Sanmenxia 472000, China)

Received date: 2019-12-17

  Online published: 2020-05-19

摘要

从白酒酒糟中获得产纤维素酶细菌,利用刚果红平板初筛、摇床发酵复筛等手段进行分离筛选,结合形态学、分子生物学鉴定及生理生化特征对菌株进行分类鉴定,并对其酶学特性进行了研究。结果表明,从酒糟中共筛选得到16株产纤维素酶菌株,其中YS10-2酶活力最高,羧甲基纤维素(carboxy methyl cellulose, CMC)酶活力为36.73 U/mL,经鉴定为巨大芽孢杆菌(Bacillus megaterium)。其胞外纤维素酶最适反应温度为50 ℃、最适pH值为5.0,具有一定的热稳定性,在弱酸性的条件下较稳定,金属离子Ca2+、Zn2+、Mg2+对酶活力有促进作用,而Cu2+和Ba2+则抑制酶活性,纤维素酶的最适反应底物为CMC。

本文引用格式

宋丽丽 , 闻格 , 霍姗浩 , 胡晓龙 , 杨旭 , 张志平 . 白酒酒糟中产纤维素酶细菌的分离筛选和酶学性质研究[J]. 食品与发酵工业, 2020 , 46(7) : 43 -49 . DOI: 10.13995/j.cnki.11-1802/ts.023111

Abstract

In order to obtain cellulase-producing bacteria from distiller′s grains, a byproduct of Chinese Baijiu, Congo red agar and shaking-flask fermentation method were used for screening. The isolate was identified by morphological and molecular biology methods combined with analysis of physicochemical characteristics, plus with the enzymatic characteristics studied. The results showed that a total of 16 cellulase-producing strains were screened, among which the strain YS10-2 possessed the highest enzyme activity of 36.73 U/mL on carboxy methyl cellulose (CMC), and was identified as Bacillus megaterium. The optimum reaction temperature and pH of the extracellular cellulase were 50 ℃ and 5.0, respectively. The cellulase was stable to both heat and weak acid. The enzyme activity was promoted by Ca2+, Zn2+, Mg2+, and inhibited by Cu2+ and Ba2+. The optimum enzymatic substrate was CMC.

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