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

Tomasz Florczak; Maurycy Daroch; Mark Wilkinson; Aneta Białkowska; Andrew Derek Bates; Marianna Turkiewicz; Lesley Ann Iwanejko

doi:10.1016/j.enzmictec.2013.03.021

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

Tomasz Florczak, Maurycy Daroch, Mark Wilkinson, Aneta Białkowska, Andrew Derek Bates, Marianna Turkiewicz, Lesley Ann Iwanejko

Research output: Contribution to journal › Article › peer-review

45 Citations (Scopus)

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 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.

Original language	English
Pages (from-to)	18-24
Number of pages	7
Journal	Enzyme and Microbial Technology
Volume	53
Issue number	1
DOIs	https://doi.org/10.1016/j.enzmictec.2013.03.021
Publication status	Published - 10 Jun 2013
Externally published	Yes

Keywords

Cold adaptation
Inverse-PCR
Lipase
Psychrophillic enzyme
Thermostability

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10.1016/j.enzmictec.2013.03.021

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Florczak, T., Daroch, M., Wilkinson, M., Białkowska, A., Bates, A. D., Turkiewicz, M., & Iwanejko, L. A. (2013). 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. Enzyme and Microbial Technology, 53(1), 18-24. https://doi.org/10.1016/j.enzmictec.2013.03.021

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title = "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 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.",

keywords = "Cold adaptation, Inverse-PCR, Lipase, Psychrophillic enzyme, Thermostability",

author = "Tomasz Florczak and Maurycy Daroch and Mark Wilkinson and Aneta Bia{\l}kowska and Bates, \{Andrew Derek\} and Marianna Turkiewicz and Iwanejko, \{Lesley Ann\}",

year = "2013",

month = jun,

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doi = "10.1016/j.enzmictec.2013.03.021",

language = "English",

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Florczak, T, Daroch, M, Wilkinson, M, Białkowska, A, Bates, AD, Turkiewicz, M & Iwanejko, LA 2013, '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', Enzyme and Microbial Technology, vol. 53, no. 1, pp. 18-24. https://doi.org/10.1016/j.enzmictec.2013.03.021

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. / Florczak, Tomasz; Daroch, Maurycy; Wilkinson, Mark et al.
In: Enzyme and Microbial Technology, Vol. 53, No. 1, 10.06.2013, p. 18-24.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - 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

AU - Florczak, Tomasz

AU - Daroch, Maurycy

AU - Wilkinson, Mark

AU - Białkowska, Aneta

AU - Bates, Andrew Derek

AU - Turkiewicz, Marianna

AU - Iwanejko, Lesley Ann

PY - 2013/6/10

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N2 - 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.

AB - 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.

KW - Cold adaptation

KW - Inverse-PCR

KW - Lipase

KW - Psychrophillic enzyme

KW - Thermostability

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DO - 10.1016/j.enzmictec.2013.03.021

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JO - Enzyme and Microbial Technology

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Florczak T, Daroch M, Wilkinson M, Białkowska A, Bates AD, Turkiewicz M et al. 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. Enzyme and Microbial Technology. 2013 Jun 10;53(1):18-24. doi: 10.1016/j.enzmictec.2013.03.021