Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69614
標題: Characterization of Codon-Optimized Recombinant Candida rugosa Lipase 5 (LIP5)
作者: Lee, L.C.
Yen, C.C.
Malmis, C.C.
Chen, L.F.
Chen, J.C.
Lee, G.C.
Shaw, J.F.
關鍵字: Candida rugosa lipase 5 (LIP5)
substrate
specificity
hydrolysis
pichia-pastoris
biochemical-characterization
substrate-specificity
multiple mutagenesis
gene family
expression
cylindracea
sequences
residues
cloning
期刊/報告no:: Journal of Agricultural and Food Chemistry, Volume 59, Issue 19, Page(s) 10693-10698.
摘要: Recombinant Candida rugosa lipase 5 (LIP5) has been functionally expressed along with other isoforms in our laboratory. However, the characterization and codon optimization of LIP5 have not been done. In this work, we characterized, codon-optimized and compared LIP5 with commercial lipase. LIP5 activity on hydrolysis of p-nitrophenyl (p-NP) butyrate was optimal at 55 degrees C as compared with 37 degrees C of the commercial lipase. Several assays were also performed to determine the substrate specificity of LIP5. p-NP butyrate (C(4)), butyryl-CoA (C(4)), cholesteryl laurate (C(12)), and N-carbobenzoxy-L-tyrosine-p-nitrophenyl ester (L-NBTNPE) were found as preferred substrates of LIP5. Interestingly, LIP5 specificity on hydrolysis of amino acid-derivative substrates was shown to be the highest among any lipase isoforms, but it had very weak preference on hydrolyzing triacylglycerol substrates. LIP5 also displays a pH-dependent maximum activity of a lipase but an esterase substrate preference in general. The characterization of LIP5 along with that of LIP1-LIP4 previously identified shows that each lipase isoform has a distinct substrate preference and catalytic activity.
URI: http://hdl.handle.net/11455/69614
ISSN: 0021-8561
文章連結: http://dx.doi.org/10.1021/jf202161a
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