检索结果-南通市图书馆

Purification and characterization of alkaline chitinase from paenibacillus pasadenensis cs0611

Chinese Journal of Catalysis 2017年第4期38卷 665-672页

作者： Xiaoxiao Guo Pei Xu Minhua Zong Wenyong Lou Laboratory of Applied Biocatalysis School of Food Science and Engineering South China University of Technology Guangzhou 510640 GuangdongChina State Key Laboratory of Pulp and Paper Engineering South China University of Technology Guangzhou 510640 Guangdong China

An extracellular chitinase produced by paenibacillus pasadenensis cs0611was purified by ammoniumsulfate precipitation,HiTrap DEAE FF and HiLoad26/600Superdex200pg column *** apparent molecular mass determined by sodium dodecyl sulfate polyacrylamide gelelectrophoresis *** optimum pH and optimum temperature of the chitinase were5.0and50°C,*** enzyme showed high stability at alkaline pH values and temperaturesbelow40°***,the metal ions Mn2+,Mg2+,and Co2+inhibited activity of the *** was active on colloidal chitin with an apparent Km of4.41mg/mL and Vmax of1.08mg/*** spectrum analysis indicated that the chitinase reacted preferentially with the glucosidicbond between GlcNAc‐*** enzymatic hydrolysate was analyzed by high‐performance liquidchromatography and thin layer chromatography,and clearly showed that a subunit of(GlcNAc)2was the main hydrolysis product.

关键词： Chitinase Purification Characterization paenibacillus pasadenensis cs0611

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

Cloning, overexpression, and characterization of a novel organic solvent-tolerant lipase from paenibacillus pasadenensis cs0611

引用

Chinese Journal of Catalysis 2018年第5期39卷 937-945页

作者： Jiaxin Gao Xiaoyang Ou Pei Xu Minhua Zong Wenyong Lou Laboratory of Applied Biocatalysis School of Food Science and EngineeringSouth China University of TechnologyGuangzhou 510640GuangdongChina State Key Laboratory of Pulp and Paper Engineering South China University of TechnologyGuangzhou 510640GuangdongChina

We found a novel lipase gene in the paenibacillus pasadenensis cs0611 *** lipase gene sequence was cloned into the pET-28a expression vector to construct a recombinant lipase protein containing 6×His tags at the C-and N-termini,***-level expression of the lipase in *** BL21(DE3)was obtained upon induction with IPTG at 20°*** recombinant lipase activity was approximately 1631-fold higher than the wild ***-tagged recombinant lipase was purified rapidly and efficiently by using Ni-charged affinity chromatography with 63.5%recovery and a purification factor of *** purified lipase was stable in a broad range of temperatures and pH values,with the optimal temperature and pH being 50°C and 7.0,*** activity was stimulated to different degrees in the presence of metal ions such as Ca2+,Mg2+,and some non-ionic *** addition,the purified lipase was activated by a series of water-miscible organic solvents such as some short carbon chain alcohols and was highly tolerant to some water-immiscible organic solvents.

关键词： Lipase paenibacillus pasadenensis cs0611 Expression Characterization Organic solvent tolerant

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：