期刊
ENZYME AND MICROBIAL TECHNOLOGY
卷 53, 期 1, 页码 18-24出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2013.03.021
关键词
Cold adaptation; Thermostability; Lipase; Psychrophillic enzyme; Inverse-PCR
资金
- National Science Center (Poland) for Scientific Research Grant [N N209231738]
- Marie Curie Host Fellowships for Early Stage Training [MEST-CT-2005-020526]
A lipase, LipG7, has been purified from the Antarctic filamentous fungus Geomyces sp. P7 which was found to be cold-adapted and able to retain/regain its activity after heat denaturation. The LipG7 exhibits 100% residual activity following 1 h incubation at 100 C whilst simultaneously showing kinetic adaptations to cold temperatures. LipG7 was also found to have industrial potential as an enantioselective biocatalyst as it is able to effectively catalyse the enantioselective transesterification of a secondary alcohol. The LipG7 coding sequence has been identified and cloned using 454 pyrosequencing of the transcriptome and inverse PCR. The LipG7 protein has been heterologously expressed in Saccharomyces cerevisiae BJ5465 and shown to exhibit the same characteristics as the native protein. (C) 2013 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据