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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38432

Title: C-Terminal Region of Candida rugosa Lipases Affects Enzyme Activity and Interfacial Activation.
Authors: Kuo-Sheng Hung
Shiow-Yi Chen
Hsu-Feng Liu
Bing-Reui Tsai
Hung-Wei Chen
Chin-Yen Huang
Ji-Long Liao
Kuang-Hui Sun
Shye-Jye Tang
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Keywords: interfacial activation
alcohol binding site
C-terminal region
Candida rugosa lipase
glycosylation
Date: 2011
Issue Date: 2016-09-01T06:08:32Z
Publisher: J. Agric. Food Chem
Abstract: Abstract: Candida rugosa contains several lipase (CRLs) genes, and CRLs show diverse enzyme activity despite being highly homologous across their entire protein family. Previous studies found that LIP4 has a high esterase activity and a low lipolytic activity and lacks interfacial activation. To investigate whether the C-terminal region of the CRLs mediates enzymatic activity, chimeras were generated in which the C-terminus of LIP4 from either residue 374, 396, 417, or 444 to residue 534 was swapped with the corresponding peptide from the isoform LIP1. A chimeric lipase containing the C-terminus from 396 to 534 of LIP1 on a LIP4 scaffold showed activity similar to that of commercial CRL on triolein, and lipolytic activity increased 2–6-fold over that of LIP4. Moreover, interfacial activation was also observed in the chimeric lipase. To improve its enzymatic properties, a novel glycosylation site was added at residue 314. The new glycosylated lipase showed improved thermostability and enhancement in enzymatic activity, indicating its potential for use in further application.
Relation: 59(10)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38432
Appears in Collections:[生命科學系] 期刊論文

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