Purification, characterisation and expression in Saccharomyces cerevisiae of LipG7 an enantioselective, cold-adapted lipase from the Antarctic filamentous fungus Geomyces sp P7 with unusual thermostability characteristics

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 kineti...

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Bibliographic Details
Published in:Enzyme and Microbial Technology
Main Authors: Florczak, Tomasz, Daroch, Maurycy, Wilkinson, Mark Charles, Bialkowska, Aneta, Bates, Andrew Derek, Turkiewicz, Marianna, Iwanejko, Lesley Ann
Other Authors: Iwanejko, LA (reprint author), Univ Liverpool, Inst Integrat Biol, Biosci Bldg,Crown St, Liverpool L69 7ZB, Merseyside, England., Tech Univ Lodz, Inst Tech Biochem, Fac Biotechnol & Food Sci, PL-90924 Lodz, Poland., Univ Liverpool, Inst Integrat Biol, Liverpool L69 7ZB, Merseyside, England., Univ Liverpool, Dept Musculoskeletal Biol, Fac Hlth & Life Sci, Inst Ageing & Chron Dis, Liverpool L69 3GA, Merseyside, England., Peking Univ, Shenzhen Grad Sch, Sch Environm & Energy, Shenzhen 518055, Peoples R China., Univ Liverpool, Inst Integrat Biol, Biosci Bldg,Crown St, Liverpool L69 7ZB, Merseyside, England.
Format: Journal/Newspaper
Language:English
Published: enzyme and microbial technology 2013
Subjects:
Cold adaptation
Thermostability
Lipase
Psychrophillic enzyme
Inverse-PCR
YARROWIA-LIPOLYTICA
ACTIVE LIPASE
EXTRACELLULAR LIPASE
MICROBIAL LIPASES
CLONING
STRAIN
GENE
CLASSIFICATION
BIOCATALYSIS
EFFICIENCY
Antarctic
The Antarctic
Antarc*
Online Access:https://hdl.handle.net/20.500.11897/222633
https://doi.org/10.1016/j.enzmictec.2013.03.021
Description
Summary: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. Biotechnology & Applied Microbiology SCI(E) EI 8 ARTICLE 1 18-24 53

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