伯克霍爾德氏菌(Burkholderia sp.)脂肪酶及其伴護子之選殖表現與應用

Both lipase gene (lp) and lipase-specific chaperone gene (lpc) of Burkholderia sp. were cloned into different expression vectors and co expressed in heterologous host Escherichia coli. After purification and dialysis, the enzymatic activity of the recombinant protein was analyzed. The results showed...

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Bibliographic Details
Published in:臺灣農業化學與食品科學 2011-12, Vol.49 (6), p.316-328
Main Authors: 彭宣融(Hsuan-Jung Peng), 董志宏(Jhih-Hong Dong), 朱燕華(Yen-Hua Chu), 凃景瑜(Ching-Yu Tu), 簡美枝(Mei-Chih Chien), 廖麗玲(Li-Ling Liaw)
Format: Article
Language:Chinese
Subjects:
Burkholderia sp
Chaperone
Lipase
Scopus
Signal peptide
Trans-esterification
TSCI
伯克霍爾德氏菌
伴護子
脂肪酶
訊息胜肽
轉酯化
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Summary:Both lipase gene (lp) and lipase-specific chaperone gene (lpc) of Burkholderia sp. were cloned into different expression vectors and co expressed in heterologous host Escherichia coli. After purification and dialysis, the enzymatic activity of the recombinant protein was analyzed. The results showed that the lipasespecific chaperone was required for the lipase activity and the signal peptide of the lipase played an important role in the lipase activity. In addition, the recombinant enzyme was an alkaline lipase with a broad range of 4-nitrophenyl ester substrates and thermo-stability. Furthermore, the recombinant lipase had excellent capability for trans-esterification in oil production.
ISSN:1605-2471