Sh. Yeo et al., SCREENING AND IDENTIFICATION OF A NOVEL LIPASE FROM BURKHOLDERIA SP. YY62 WHICH HYDROLYZES T-BUTYL ESTERS EFFECTIVELY, Journal of General and Applied Microbiology, 44(2), 1998, pp. 147-152
Fatty acid esters composed of sterically hindered alcohol are very poo
r substrates for known lipases. In order to obtain a novel lipase, t-b
utyl octanoate (TBO) was selected as a model substrate to screen for b
acteria-producing lipase(s) which can preferentially hydrolyze bulky e
sters. Of 279 strains isolated from 350 soil samples based an the abil
ity to grow with TBO as a sole carbon source, one strain (YY62) was ch
osen for its strong TBO-hydrolyzing activity. Strain YY62 is a Gram-ne
gative motile rod and was identified as Burkholderia sp. from the taxo
nomic characters and phylogenetic analysis of 16S rDNA nucleotide sequ
ences. Using the activity ratio between TBO and p-nitrophenyl acetate
as a measure for preference to bulky esters, we confirmed that the lip
ase of strain YY62 was 100-fold superior to commercial lipases in term
s of TBO-hydrolyzing activity.