Document Detail


C-Terminal Region of Candida rugosa Lipases Affects Enzyme Activity and Interfacial Activation.
MedLine Citation:
PMID:  21504227     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Candida rugosa contains several lipase (CRLs) genes, and CRLs show diverse enzyme activity despite highly homologous across their entire protein family. In our previous studies, we found that LIP4 has a high esterase activity, a low lipolytic activity, and lacks of interfacial activation. To investigate whether the C-terminal region of the CRLs mediates enzymatic activity, we generated chimeras 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 folds over LIP4. Moreover, interfacial activation was also observed in the chimeric lipase. To improve its enzymatic properties, we added a novel glycosylation site at residue 314. The new glycosylated lipase showed improved thermostability and enhancement in enzymatic activity, indicating its potential for use in further application.
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
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-4-19
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  -     ISSN:  1520-5118     ISO Abbreviation:  -     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-4-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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