Document Detail

C-Terminal Region of Candida rugosa Lipases Affects Enzyme Activity and Interfacial Activation.
MedLine Citation:
PMID:  21504227     Owner:  NLM     Status:  Publisher    
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.
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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