文献类型：期刊文献

英文题名：High level expression of Saccharomyces cerevisiae chitinase (ScCTS1) in Pichia pastoris for degrading chitin

作者：Zhao Youxi[1,2];Jiang Huihui[1];Rao Zhiming[1];Ji Yizhi[2];Cheng Yanling[2];Ma Yanhe[3]

第一作者：赵有玺;Zhao Youxi

通讯作者：Rao, ZM[1]

机构：[1]Jiangnan Univ, Sch Biotechnol, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Peoples R China;[2]Beijing Union Univ, Biochem Engn Coll, Beijing Key Lab Biomass Waste Resource Utilizat, Beijing 100023, Peoples R China;[3]Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100101, Peoples R China

第一机构：Jiangnan Univ, Sch Biotechnol, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Peoples R China

通讯机构：[1]corresponding author), Jiangnan Univ, Sch Biotechnol, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Peoples R China.

年份：2015

卷号：8

期号：5

起止页码：142-150

外文期刊名：INTERNATIONAL JOURNAL OF AGRICULTURAL AND BIOLOGICAL ENGINEERING

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000365459600017)】；

基金：This work was supported by the General Project of Beijing Municipal Education Commission (No. SQKM201311417003), Beijing Excellent Talents Cultivation Project (No. 2012D005022000007) and Ministry of Science and Technology "863 Plan" Project (No. 2015AA020202).

语种：英文

外文关键词：chitinases; heterologous expression; Saccharomyces cerevisiae; pichia pastoris; biotechnology

摘要：Chitin is the second most abundant renewable biopolymer in the world. Chitinases play important roles in the degradation of chitin. Chitinases are produced by different organisms for different purposes, which are widely expressed in the three domains of life, ranging from archaea, bacteria, to fungi, yeasts, plants, insects, and even vertebrates. But there are few reports about Saccharomyces cerevisiae chitinase (ScCTS1). The aim of this study was to realize the high level expression of ScCTS1. The ScCTS1 was cloned into the expression vector pPIC9K. The recombinant plasmid was linearized and transformed into competent Pichia pastoris GS115. After screening by G418 plate, the fermentation conditions were optimized. Ultimately, under the optimal fermentation conditions, ScCTS1 enzymatic activity reached up to 94.6 U/mL. This paper presents the first report on the heterologous expression of a full-length ScCTS1 with considerably high activity. The work will not only make a great stride towards its potential applications in biotechnology, but also facilitate elucidating the precise mechanism of yeast cell division.