TY - JOUR
T1 - Kinetic study of asymmetric hydrolysis of dimethyl 3-(4-fluorophenyl) glutarate using novozym 435
AU - Ma, Yan
AU - Liu, Wei Ming
AU - Huang, He
AU - Li, Shuang
AU - Hu, Yi
N1 - Publisher Copyright:
©, 2015, Zhejiang University. All right reserved.
PY - 2015/2/1
Y1 - 2015/2/1
N2 - Immobilized Candida antarctica lipase B (Novozym 435) was used to catalyze the asymmetric hydrolysis of dimethyl 3-(4-fluorophenyl)glutarate (3-DFG) in an aqueous system containing methyl tert-butyl ether (MTBE) as cosolvent. The present work put emphasis on the kinetic study of the asymmetric hydrolysis reaction. The effects of rotation speed, enzyme loading, concentrations of substrate and product on the reaction were investigated. The optimal rotation speed was 200 r·min-1, and the reaction was free from intra-particle diffusion limitations. The inhibitions of substrate (3-DFG) and product (3-MFG) were excluded which both displayed no decline on the activity of Novozym 435 at elevated concentrations within the given range. In addition, methanol, a byproduct of the reaction, inhibited the activity of Novozym 435 following a competitive inhibition pattern. The kinetic constants were obtained through non-linear regression, with values of Km 0.24 mol·L-1, Ki 0.39 mol·L-1, Vmax 2.39 mmol·L-1·h-1, respectively.
AB - Immobilized Candida antarctica lipase B (Novozym 435) was used to catalyze the asymmetric hydrolysis of dimethyl 3-(4-fluorophenyl)glutarate (3-DFG) in an aqueous system containing methyl tert-butyl ether (MTBE) as cosolvent. The present work put emphasis on the kinetic study of the asymmetric hydrolysis reaction. The effects of rotation speed, enzyme loading, concentrations of substrate and product on the reaction were investigated. The optimal rotation speed was 200 r·min-1, and the reaction was free from intra-particle diffusion limitations. The inhibitions of substrate (3-DFG) and product (3-MFG) were excluded which both displayed no decline on the activity of Novozym 435 at elevated concentrations within the given range. In addition, methanol, a byproduct of the reaction, inhibited the activity of Novozym 435 following a competitive inhibition pattern. The kinetic constants were obtained through non-linear regression, with values of Km 0.24 mol·L-1, Ki 0.39 mol·L-1, Vmax 2.39 mmol·L-1·h-1, respectively.
KW - Asymmetric hydrolysis
KW - Inhibition mechanism
KW - Kinetic
KW - Novozym 435
UR - http://www.scopus.com/inward/record.url?scp=84925651726&partnerID=8YFLogxK
U2 - 10.3969/j.issn.1003-9015.2015.01.022
DO - 10.3969/j.issn.1003-9015.2015.01.022
M3 - 文章
AN - SCOPUS:84925651726
SN - 1003-9015
VL - 29
SP - 145
EP - 150
JO - Gao Xiao Hua Xue Gong Cheng Xue Bao/Journal of Chemical Engineering of Chinese Universities
JF - Gao Xiao Hua Xue Gong Cheng Xue Bao/Journal of Chemical Engineering of Chinese Universities
IS - 1
ER -