Expression of Candida antarctica lipase B on yeast surface and synthesis of ethyl hexanoate catalyzed by CALB / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 673-678, 2008.
Article
in Chinese
| WPRIM
| ID: wpr-342852
ABSTRACT
Short-chain esters play a significant role in the food industry as flavor and aroma constituents. Candida antarctica lipase B (CALB) is one of the most effective catalysts for organic synthesis. We constructed a CALB-displaying yeast whole-cell biocatalyst and applied it to esterification from caproic acid and ethanol. CALB was fused with the alpha-agglutinin C-terminal and the signal peptide of Glucoamylase in pICAS, a yeast surface display vector, to construct plasmid pICAS-CALB. An extremely Asn-rich linker, named celAL was inserted in the Xho I of pICAS-CALB to construct plasmid pICAS-celAL-CALB. The fused gene was under the control of GAPDH promoter. After incubated at 30 degrees C for 96 h the lipase hydrolytic activity of the yeast whole cells reached a plateau, 26.26 u/(g x dry cell). In nonaqeous media, the yield of 98.0% ethyl hexanoate was obtained after 24 h esterification from caproic acid and ethanol (the molar ratio of caproic acid ethanol = 1 1.25) using lyophilized CALB displaying yeast whole cells.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Saccharomyces cerevisiae
/
Candida
/
Caproates
/
Fungal Proteins
/
Genetic Engineering
/
Cloning, Molecular
/
Biocatalysis
/
Genetics
/
Lipase
/
Metabolism
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2008
Type:
Article
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