Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63

Yang, Jiangke; Guo, Daoyi; Yan, Yunjun

doi:10.1016/j.molcatb.2006.12.007

Cited by 78 publications

(37 citation statements)

References 29 publications

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“…Rathi et al (2000Rathi et al ( , 2001 reported that optimum activity of lipase from Burkholderia cepacia was at 90 °C and at pH 11. Yang et al (2007) found that the optimal temperature 70 °C and pH 8.0 for lipase from Burkholderia cepacia strain G63, and kept stable at a temperature range of 40-70 °C, after incubation at 70 °C for 10 h it remained 86.1% of its activity. Liu et al (2006) reported that the optimal reaction conditions of lipase from Burkholderia sp.…”

Section: Discussionmentioning

confidence: 93%

“…Of these, the important ones are: Achromobacter, Alcaligenes, Arthrobacter, Bacillus, Burkholderia, Chromobacterium and Pseudomonas (Gupta et al, 2004). Several kinds of lipases originating from Burkholderia species have been identified and their enzymatic properties and crystal structures have been elucidated (Rathi et al, 2001;Mandrich et al, 2005;Park et al, 2007;Yang et al, 2007). Because of their preference for the hydrolysis of triglycerides with a long chain length (greater than C8), excellent enantioselectivity, transesterification, esterification and tolerance to solvents and high temperature, Burkholderia lipases were extensively studied during the past two decades for industrial use (Maury et al, 2005;Orcaire et al, 2006;Fernades et al, 2007;Park et al, 2007;Yu et al, 2007;Li et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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A novel alkaline and low-temperature lipase ofBurkholderia cepacia isolated from Bohai in China for detergent formulation

Wang

Liu

et al. 2009

Ann. Microbiol.

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The bacterial strain LP08 was isolated from soil collected from bay of Bohai, China. The sequence of 16S rDNA of strain LP08 showed 99% homology to Burkholderia cepacia. The lipase from Burkholderia cepacia LP08 was purified by ammonium sulphate precipitation, ion exchange chromatography and Sephadex G-75 chromatography. The characterization of the lipase exhibited maximum activity at 30 °C and pH 9.0. The lipase retained 63, 66, 74, and 95% of its maximum activity at 10, 15, 20 and 25 °C respectively. The lipase activity was promoted in the presence of commercial detergent, sodium cholate, sodium taurocholate, glycerine and NaCl, while was little inhibited in the presence of TritonX-100, Tween-20, Tween-80, SDS, saponin. The present lipase was highly stable towards oxidizing agents and was stable after 1 h at 25 °C in the presence of hydrogen peroxide, sodium hypochlorite and sodium perborate. The results suggest that the lipase from Burkholderia cepacia LP08 showed good potential for application in the detergent formulation.

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Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

A novel alkaline and low-temperature lipase ofBurkholderia cepacia isolated from Bohai in China for detergent formulation

Wang

Liu

et al. 2009

Ann. Microbiol.

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“…The protein encoded by lip B was a molecular chaperone of Lip A, helping Lip A fold and secrete correctly (Steen et al, 1991). The nucleotide sequence of lip A was aligned with lip A sequences from P. cepacia KWI-56, B. cepacia G63, and other Burkholderia strains (lizumi et al, 1990;Yang et al, 2007). There is about 90% sequence identity among these genes.…”

Section: Gene Cloning Of S31 Lipasementioning

confidence: 99%

Identification of bacteria producing a thermophilic lipase with positional non-specificity and characterization of the lipase

Lü

Wang

et al. 2009

Ann. Microbiol.

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-A bacterial isolate producing lipase, named S31, was isolated from soil and identified as a strain of Burkholderia cepacia. S31 produced high activity of lipase which reached a maximum of 226.1 U/ml by fermenting at 30 °C for 60 h under the induction of olive oil. After purification, the lipase showed a single band of about 35 kDa in SDS-PAGE. The optimum temperature of the lipase was 70 °C and the optimum pH was 9.0. S31 lipase was stable at 40-70 °C and pH 0.5-10.0, as well as in several organic solvents, such as methanol, n-hexane, n-butanol, toluene and ethyl acetate. The presence of some metal ions (Ca 2+ , Mn 2+ , K + , Na + and Mg 2+ ) could activate the enzyme whereas Fe 2+ and Cu 2+ were found to be inhibitory. The lipase could cleave all of the three ester bonds of triglycerides. We conclude that S31 lipase is an alkaline lipase with a variety of highly desirable characteristics for research and industrial application.

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“…Among them, Burkholderia cepacia lipase (BCL) is a versatile one and has been widely used in organic synthesis, biodiesel preparation, biodegradation and many other reactions in aqueous and non-aqueous phases [3][4][5]. Recently, enzymatic chiral resolution by lipases has generated huge interest due to the merits of it having fewer byproducts, a simple operation and environmental friendliness [6,7].…”

Section: Introductionmentioning

confidence: 99%

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

Cui

et al. 2018

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Abstract:A kind of pH-responsive particle was synthesized using modified pullulan polysaccharide. The synthesized particle possessed a series of merits, such as good dispersity, chemical stability and variability of particle size, making it a suitable carrier for enzyme immobilization. Then, Burkholderia cepacia lipase (BCL), a promising biocatalyst in transesterification reaction, was immobilized on the synthesized particle. The highest catalytic activity and immobilization efficiency were achieved at pH 6.5 because the particle size was obviously enlarged and correspondingly the adsorption surface for BCL was significantly increased. The immobilization enzyme loading was further optimized, and the derivative lipase was applied in chiral resolution. Under the optimal reaction conditions, the immobilized BCL showed a very good performance and significantly shortened the reaction equilibrium time from 30 h of the free lipase to 2 h with a conversion rate of 50.0% and ee s at 99.2%. The immobilized lipase also exhibited good operational stability; after being used for 10 cycles, it still retained over 80% of its original activity. Moreover, it could keep more than 80% activity after storage for 20 days at room temperature in a dry environment. In addition, to learn the potential mechanism, the morphology of the particles and the immobilized lipase were both characterized with a scanning electron microscope and confocal laser scanning microscopy. It was found that the enlarged spherical surface of the particle in low pH values probably led to high immobilized efficiency, resulting in the improvement of enantioselectivity activity in chiral resolution.

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Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63

Cited by 78 publications

References 29 publications

A novel alkaline and low-temperature lipase ofBurkholderia cepacia isolated from Bohai in China for detergent formulation

A novel alkaline and low-temperature lipase ofBurkholderia cepacia isolated from Bohai in China for detergent formulation

Identification of bacteria producing a thermophilic lipase with positional non-specificity and characterization of the lipase

Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution

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