Production of (S)-4-chloro-3-hydroxybutyrate by microbial resolution using hydrolase from Rhizobium sp. DS-S-51.
(S)-4-Chloro-3-hydroxybutyrate (CHB) is essential for the synthesis of biologically and pharmacologically important compounds. Rhizobium sp. DS-S-51 isolated from soil samples showed hydrolytic activity toward (R)-CHB in the racemate to (R)-3-hydroxy-gamma-butyrolactone (HL) under a simple composition of the reaction. Residual (S)-CHB was obtained with high optical purity. The gene encoding the enzyme concerned, designated CHB hydrolase, was isolated from DS-S-51, and the gene was highly expressed in Escherichia coli JM109. When the resolution of racemic methyl CHB (CHBM) as a substrate was performed using this recombinant cell, JM109 (pKK-R1), the hydrolytic activity was found to be 40-fold greater than that of DS-S-51, and the maximum concentration of the substrate added increased 2-fold. Moreover, (R)-HL was also obtained without decreasing the optical purity compared with that when (R)-CHBM was used as a substrate.
Nakagawa
Atsushi
A
Research Laboratories of DAISO Co., Ltd., 9 Otakasu-cho, Amagasaki, Hyogo 660-0842, Japan.
Suzuki
Takahiro
T
Kato
Ko
K
Shinmyo
Atsuhiko
A
Suzuki
Toshio
T
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D006885:Hydroxybutyrates / Q000138:chemical synthesis* / Q000737:chemistry; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012231:Rhizobium / Q000201:enzymology* / Q000235:genetics; D012988:Soil Microbiology
C511345:4-chloro-3-hydroxybutyric acid; D001426:Bacterial Proteins; D006885:Hydroxybutyrates; D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases