Isolation and characterization of Acinetobacter sp. ES-1 excreting a lipase with high enantioselectivity for (S)-ketoprofen ethyl ester.
A new Acinetobacter sp. ES-1, grown on triolein, tryptone and Triton X-100, excreted a lipase that hydrolyzed 10 mM (R,S)-ketoprofen ethyl ester into (S)-ketoprofen. The crude lipase had an activity of 10 U ml(-1) and, at 30 degrees C and pH 7 over 48 h, gave a conversion yield of 35% with an enantiomeric excess for the product 96%.
Lee
Kwang-Woo
KW
Department of Genetic Engineering, College of Natural Sciences, Kyungpook National University, Daegu, 702-701, S. Korea.
Shin
Gab-Sang
GS
Bae
Hyun-Ae
HA
Shin
Hyun-Dong
HD
Lee
Yong-Hyun
YH
D000150:Acinetobacter / Q000145:classification / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification*; D004789:Enzyme Activation; D004952:Esters; D006868:Hydrolysis; D007536:Isomerism; D007660:Ketoprofen / Q000737:chemistry*; D008049:Lipase / Q000032:analysis / Q000096:biosynthesis* / Q000737:chemistry*; D012722:Sewage / Q000382:microbiology*; D013045:Species Specificity; D013379:Substrate Specificity
D004952:Esters; D012722:Sewage; D007660:Ketoprofen; D008049:Lipase