Gene cloning and catalytic characterization of cold-adapted lipase of Photobacterium sp. MA1-3 isolated from blood clam

Kim, Young Ok; Khosasih, Vivia; Nam, Bo‐Hye; Lee, Sang-Jun; Suwanto, Antonius; Kim, Hyung Kwoun

doi:10.1016/j.jbiosc.2012.06.013

Cited by 19 publications

(15 citation statements)

References 26 publications

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“…Therefore, we expressed lipE5 using the E. coli BL21(DE3)/pET22b(+) expression system, as reported before for other cold-active lipases [27,28], and characterized its activity against p-nitrophenyl caproate. The enzyme showed a high specific activity between 15 and 25 • C and an optimal activity at 25 • C at pH 8 and the retention of 35% of its maximum activity at 10 • C. Specific activities for other lipases described as cold-active enzymes have been reported with optimal activities between 10 and 45 • C [26,[29][30][31][32][33]. Therefore, these results support the finding of a novel cold-active lipase.…”

Section: Discussionsupporting

confidence: 78%

Identification of lipase encoding genes from Antarctic seawater bacteria using degenerate primers: Expression of a cold-active lipase with high specific activity

Parra

Espina

Devia

et al. 2015

Enzyme and Microbial Technology

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Section: Discussionsupporting

confidence: 78%

Identification of lipase encoding genes from Antarctic seawater bacteria using degenerate primers: Expression of a cold-active lipase with high specific activity

Parra

Espina

Devia

et al. 2015

Enzyme and Microbial Technology

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“…Recently, research on cold-adapted lipase has gone down a new direction. Young Ok Kim et al [26] reported cold-adapted lipase of Photobacterium sp. MA1-3 isolated from blood clam and MA1-3 lipase showed optimum activity at 45°C, pH 8.5.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Cold-Adapted Lipase from Oceanobacillus Strain PT-11

et al. 2014

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We isolated a moderately halophilic lipase-producing bacterium from the saline soil. Based on the morphological, physiological, chemotaxonomic and phylogenetic analysis, the isolate PT-11 was postulated to be a novel species identified as Oceanobacillus rekensis PT-11. The lipase was purified 2.50-fold by Q-Sepharose FF and SP-Sepharose FF chromatography and its molecular mass was estimated to be 23.5 kDa by SDS-PAGE. It was highly active over the broad temperature ranging from 10 to 35°C and showed up to 80% of the maximum activity at 10°C indicating the lipase to be a typical cold-adapted enzyme. The enzyme activity was slightly enhanced by Na+, Li+ and K+. Incubation with detergents, such as Tween-20 and Tween-80, slightly inhibited the enzyme activity; while Triton X-100decreased the enzyme activity. The enzyme was fairly stable in the presence of long-chain alcohols but was highly denatured in hydrophilic solvents such as acetone or short-chain alcohols (C1–C3).

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“…Low values of E A are typical of coldactive lipases from different organisms such as Psychrobacter sp. (Parra et al 2008), Antarctic Bacillus pumilus strains (Litantra et al 2013) and Photocacterium strain (Kim et al 2012), which displayed E A of 23, 18 and 11.3 kJ mol −1 , in the conditions of the respective studies. In comparison, CaLIP5, the previously identified cold-active lipase belonging to the CaLA superfamily, showed higher activation energy for hydrolysis (36 kJ mol −1 ), in a temperature range of 5-25°C above which its enzymatic rate decreased (Lan et al 2011).…”

Section: Discussionmentioning

confidence: 94%

Homologous yeast lipases/acyltransferases exhibit remarkable cold-active properties

Neang

Subileau

Perrier

et al. 2014

Appl Microbiol Biotechnol

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Lipases/acyltransferases catalyse acyltransfer to various nucleophiles preferentially to hydrolysis even in aqueous media with high thermodynamic activity of water (a w >0.9). Characterization of hydrolysis and acyltransfer activities in a large range of temperature (5 to 80 °C) of secreted recombinant homologous lipases of the Pseudozyma antarctica lipase A superfamily (CaLA) expressed in Pichia pastoris, enlighten the exceptional cold-activity of two remarkable lipases/acyltransferases: CpLIP2 from Candida parapsilosis and CtroL4 from Candida tropicalis. The activation energy of the reactions catalysed by CpLIP2 and CtroL4 was 18-23 kJ mol(-1) for hydrolysis and less than 15 kJ mol(-1) for transesterification between 5 and 35 °C, while it was respectively 43 and 47 kJ mol(-1) with the thermostable CaLA. A remarkable consequence is the high rate of the reactions catalysed by CpLIP2 and CtroL4 at very low temperatures, with CpLIP2 displaying at 5 °C 65 % of its alcoholysis activity and 45 % of its hydrolysis activity at 30 °C. These results suggest that, within the CaLA superfamily and its homologous subgroups, common structural determinants might allow both acyltransfer and cold-active properties. Such biocatalysts are of great interest for the efficient synthesis or functionalization of temperature-sensitive lipid derivatives, or more generally to lessen the environmental impact of biocatalytic processes.

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Gene cloning and catalytic characterization of cold-adapted lipase of Photobacterium sp. MA1-3 isolated from blood clam

Cited by 19 publications

References 26 publications

Identification of lipase encoding genes from Antarctic seawater bacteria using degenerate primers: Expression of a cold-active lipase with high specific activity

Identification of lipase encoding genes from Antarctic seawater bacteria using degenerate primers: Expression of a cold-active lipase with high specific activity

Purification and Characterization of a Cold-Adapted Lipase from Oceanobacillus Strain PT-11

Homologous yeast lipases/acyltransferases exhibit remarkable cold-active properties

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