title: Screening and identification of a novel lipase from Burkholderia sp. YY62 which hydrolyzes t-butyl esters effectively.
abstract: Fatty acid esters composed of sterically hindered alcohol are very poor substrates for known lipases. In order to obtain a novel lipase, t-butyl octanoate (TBO) was selected as a model substrate to screen for bacteria-producing lipase(s) which can preferentially hydrolyze bulky esters. Of 279 strains isolated from 350 soil samples based on the ability to grow with TBO as a sole carbon source, one strain (YY62) was chosen for its strong TBO-hydrolyzing activity. Strain YY62 is a Gram-negative motile rod and was identified as Burkholderia sp. from the taxonomic characters and phylogenetic analysis of 16S rDNA nucleotide sequences. Using the activity ratio between TBO and p-nitrophenyl acetate as a measure for preference to bulky esters, we confirmed that the lipase of strain YY62 was 100-fold superior to commercial lipases in terms of TBO-hydrolyzing activity.
authors.affiliation: Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita 565-0871, Japan.
authors.forename: Soo-Hwan
authors.initials: SH
authors.lastname: Yeo
authors.forename: Takuya
authors.initials: T
authors.lastname: Nihira
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Yamada