Wheat germ lipase catalyzed kinetic resolution of secondary alcohols in non-aqueous media.
The lipase from wheat germ was used for the kinetic resolution of secondary alcohols. It has the opposite enantioselectivity against the Kazlauskas rule and acts as an anti-Kazlauskas catalyst. The effect of initial water activity, organic solvent, acyl donor and temperature were investigated. Wheat germ lipase had a high activity and enantioselectivity only in n-hexane with a high initial water activity (alpha(w) = 0.97), especially with 1-phenylethanol (C 32%, E > 200). Its performance changed little with the chain length of acyl donor and temperature.
Xia
Xiaole
X
School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
Wang
Yong-Hua
YH
Yang
Bo
B
Wang
Xiaoning
X
D000438:Alcohols / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009930:Organic Chemicals; D012997:Solvents / Q000378:metabolism*; D013696:Temperature; D014908:Triticum / Q000201:enzymology*; D014867:Water
D000438:Alcohols; D009930:Organic Chemicals; D012997:Solvents; D014867:Water; D008049:Lipase