Isolation of lipase producer and its performance in enantioselective hydrolysis of glycidyl butyrate.
A racemic glycidyl butyrate resolving strain, preliminarily identified as a Rhizopus sp., had been isolated from soil. Its extracellular lipase was found to enantioselectively hydrolyze the (S)-enantiomer of the chiral ester, with optimal activities at pH 5.3 and 42 degrees C. Higher enantioselectivity of the enzyme was observed at lower temperatures, while the best enantioselectivity was obtained at pH 5.5-6.0, with an E value (enantiomeric ratio) of 57.
Jia
Shi-Ying
SY
Laboratory of Biocatalysis, PO Box 283, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, P. R. China.
Xu
Jian-He
JH
Li
Qing Shan
QS
Yu
Jun Tang
JT
D002087:Butyrates / Q000378:metabolism*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008049:Lipase / Q000378:metabolism*; D025282:Mycelium / Q000145:classification / Q000378:metabolism; D015203:Reproducibility of Results; D012233:Rhizopus / Q000145:classification* / Q000201:enzymology*; D012680:Sensitivity and Specificity; D012988:Soil Microbiology; D013045:Species Specificity; D013237:Stereoisomerism; D013696:Temperature
D002087:Butyrates; D008049:Lipase