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.

Abstract:

: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 1h 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.

journal_name

Enzyme Microb Technol

authors

Florczak T,Daroch M,Wilkinson MC,Białkowska A,Bates AD,Turkiewicz M,Iwanejko LA

doi

10.1016/j.enzmictec.2013.03.021

subject

Has Abstract

pub_date

2013-06-10 00:00:00

pages

18-24

issue

1

eissn

0141-0229

issn

1879-0909

pii

S0141-0229(13)00078-1

journal_volume

53

pub_type

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