• Korean Journal of Environmental Biology
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• v.28 no.2
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• pp.95-100
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• 2010

Burkholderia cepacia PBSA-7, Bacillus licheniformis PBSA-8 and Burkholderia sp. PBSA-9 previously collected from Korea soil (Joo and Kim, 2009) were analyzed for the presence of genes encoding proteins operative in the degradation of poly(butylene succinate-co-butylene adipate; PBSA). Polymerase chain reaction analyses revealed a 1.5 kb fragment of the lipase gene (lip A) in B. cepacia PBSA-7 and Burkholderia sp. PBSA-9, while B. licheniformis PBSA-8 harbored the same gene fragment at 600 bp. The three strains possessed "Gly-X1-Ser-X2-Gly" and "Ala-X1-Ser-X2-Gly" lipase sequence regions. Burkholderia sp. PBSA-7 lip A displayed 36~40% homology with the family 1-1 lipases and 82~92% homology with the family 1-5. Burkholderia sp. PBSA-8 lip A was 64~65% homologous with the subfamily 1-4 lipases, but displayed no homology with the subfamily 1-5 lipases. Burkholderia sp. PBSA-9 lip A displayed 35~37% homology with the family I1 lipases and 83~94% homology with the family I2 lipases, similar to Burkholderia sp. PBSA-7.

• Journal of Microbiology and Biotechnology
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• v.25 no.12
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• pp.2024-2033
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• 2015

A gene encoding lipolytic enzyme, lip7-3, was isolated from Bacillus sp. W130-35 isolated from a tidal mud flat. The gene encoded a protein of 215 amino acids with a signal peptide composed of 34 amino acid residues. Lip7-3 belonged to the family I.4 lipase and showed its maximal activity at pH 9.0 and 60℃. Its activity increased in the presence of 30% methanol and, remarkably, increased as well to 154.6% in the presence of Ca²⁺. Lip7-3 preferred p-nitrophenyl octanoate (C8) as a substrate and exhibited broad specificity for short- to long- chain fatty acid esters. Additionally, Lip7-3 showed a low degree of enantioselectivity for an S-enantiomer (e.g., (S)-methyl-3-hydroxy-2-methylpropionate). It efficiently hydrolyzed glyceryl tributyrate, but did not hydrolyze glyceryl trioleate, fish oil, or olive oil. Its substrate specificity and activation by the solvent might offer a merit to the biotechnological enzyme applications like transesterification in the production of biodiesel.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.4
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• pp.458-462
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• 2005

The study was aimed at detecting polymorphism of the fifth intron in lipoprotein lipase (LPL) gene and analyzing association between the polymorphism and productive traits. A pair of primers was designed for amplifying the fifth intron. Sequence analysis indicated that a G1171C substitution existed in Large White breed. The mutation was detected by PCR-AfaI-RFLP. Polymorphism analysis in a pig resource family showed that there existed significant effects on carcass and meat quality traits. Thoraxwaist fat thickness of BB genotype was significantly higher (14.2%, p<0.05) than that of AA on carcass traits, while BB genotype was significantly lower (3.6% p<0.01, 4.1% p<0.01; 2.3% p<0.01, 1.9% p<0.01; 1.8% p<0.01, 1.4% p<0.05) than AA and AB genotype in pH of m. Longissimus Dorsi (LD), m. Biceps Femoris (BF), m. Semipinali Capitis (SC). The allelic frequencies were also significantly different between indigenous Chinese breeds and exotic breeds. Data analyzed revealed that the mutation locus affected production traits mostly by additive effects. Based on these results, it is necessary to do more studies on LPL gene before making the LPL locus into the application of marker-assisted selection (MAS) programs.