| Title : Directed evolution of Aspergillus oryzae lipase for the efficient resolution of (R,S)-ethyl-2-(4-hydroxyphenoxy) propanoate - Zhang_2020_Bioprocess.Biosyst.Eng_43_2131 |
| Author(s) : Zhang M , Li Q , Lan X , Li X , Zhang Y , Wang Z , Zheng J |
| Ref : Bioprocess Biosyst Eng , 43 :2131 , 2020 |
| Abstract : Aspergillus oryzae lipase (AOL) is a potential biocatalyst for industrial application. In this study, a mutant lipase AOL-3(F38N/V230R) was screened through two rounds of directed evolution, resulting in a fourfold increase in lipase activity, and threefold in catalytic efficiency (k(cat)/K(m)), while maintaining its excellent stereoselectivity. AOL-3(F38N/V230R) enzyme activity was maximum at pH 7.5 and also at 40 degreesC. And compared with wild-type AOL-3, AOL-3(F38N/V230R) preferentially hydrolyzed the fatty acid ethyl ester carbon chain length from C4 to C6-C10. In the same catalytic reaction conditions, the conversion of (R,S)-ethyl-2-(4-hydroxyphenoxy) propanoate ((R,S)-EHPP) by AOL-3(F38N/V230R) can be increased 169.7% compared to the original enzyme. The e.e.(s) of (R,S)-EHPP achieved 99.4% and conversion about 50.2% with E value being 829.0. Therefore, AOL-3(F38N/V230R) was a potential biocatalyst for obtaining key chiral compounds for aryloxyphenoxy propionate (APP) herbicides. |
| ESTHER : Zhang_2020_Bioprocess.Biosyst.Eng_43_2131 |
| PubMedSearch : Zhang_2020_Bioprocess.Biosyst.Eng_43_2131 |
| PubMedID: 32959146 |
| Gene_locus related to this paper: aspor-TGLA |
| Gene_locus related to this paper: aspor-TGLA |
Zhang M, Li Q, Lan X, Li X, Zhang Y, Wang Z, Zheng J (2020)
Directed evolution of Aspergillus oryzae lipase for the efficient resolution of (R,S)-ethyl-2-(4-hydroxyphenoxy) propanoate
Bioprocess Biosyst Eng
43 :2131
Zhang M, Li Q, Lan X, Li X, Zhang Y, Wang Z, Zheng J (2020)
Bioprocess Biosyst Eng
43 :2131