Journal article

Heterologous expression of an extra-cellular lipase from the basidiomycete Pleurotus sapidus


Authors listKrügener, S; Zelena, K; Zorn, H; Nimtz, M; Berger, RG

Publication year2009

Pages16-21

JournalJournal of Molecular Catalysis B: Enzymatic

Volume number57

Issue number1-4

ISSN1381-1177

DOI Linkhttps://doi.org/10.1016/j.molcatb.2008.06.014

PublisherElsevier


Abstract
The 1641 bp cDNA encoding an extra-cellular lipase of the basidiomycete Pleurotus sapidus (Lip2) was cloned from a cDNA library. Expression of the cDNA in Escherichia coli, with and without signal sequence, led to the production of recombinant Lip2, mainly as inclusion bodies with low catalytic activity. Refolding yielded catalytically active protein. A C-terminal His tag was used for purification and immunochemical detection. The recombinant lipase hydrolysed xanthophyll esters with high efficiency, and omitting the signal sequence did not alter the catalytic properties. The P. sapidus lipase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus characterised on the molecular level and expressed in a manageable host.



Authors/Editors




Citation Styles

Harvard Citation styleKrügener, S., Zelena, K., Zorn, H., Nimtz, M. and Berger, R. (2009) Heterologous expression of an extra-cellular lipase from the basidiomycete Pleurotus sapidus, Journal of Molecular Catalysis B: Enzymatic, 57(1-4), pp. 16-21. https://doi.org/10.1016/j.molcatb.2008.06.014

APA Citation styleKrügener, S., Zelena, K., Zorn, H., Nimtz, M., & Berger, R. (2009). Heterologous expression of an extra-cellular lipase from the basidiomycete Pleurotus sapidus. Journal of Molecular Catalysis B: Enzymatic. 57(1-4), 16-21. https://doi.org/10.1016/j.molcatb.2008.06.014


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