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 Technoljournal_title
Enzyme and microbial technologyauthors
Florczak T,Daroch M,Wilkinson MC,Białkowska A,Bates AD,Turkiewicz M,Iwanejko LAdoi
10.1016/j.enzmictec.2013.03.021subject
Has Abstractpub_date
2013-06-10 00:00:00pages
18-24issue
1eissn
0141-0229issn
1879-0909pii
S0141-0229(13)00078-1journal_volume
53pub_type
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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