Journal article
Authors list: Krügener, S; Zelena, K; Zorn, H; Nimtz, M; Berger, RG
Publication year: 2009
Pages: 16-21
Journal: Journal of Molecular Catalysis B: Enzymatic
Volume number: 57
Issue number: 1-4
ISSN: 1381-1177
DOI Link: https://doi.org/10.1016/j.molcatb.2008.06.014
Publisher: Elsevier
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.
Citation Styles
Harvard Citation style: Krügener, 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 style: Krügener, 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