Purification and properties of the alkaline lipase from <i>Burkholderia cepacia</i> A.T.C.C. 25609

Dalal, Sohel; Singh, Pradeep Kumar; Raghava, Smita; Rawat, Seema; Gupta, Munishwar N.

doi:10.1042/ba20070186

Cited by 36 publications

(20 citation statements)

References 44 publications

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“…Due to the surface hydrophobic patches on esterases, ammonium sulfate precipitation followed by HIC can be considered as an effective two-step purification strategy for esterases [21]. …”

Section: Resultsmentioning

confidence: 99%

Esterase Active in Polar Organic Solvents from the YeastPseudozymasp. NII 08165

et al. 2014

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Esterases/lipases active in water miscible solvents are highly desired in biocatalysis where substrate solubility is limited and also when the solvent is desired as an acyl acceptor in transesterification reactions, as with the case of biodiesel production. We have isolated an esterase from the glycolipid producing yeast-Pseudozyma sp. NII 08165 which in its crude form was alkali active, thermo stable, halo tolerant and also capable of acting in presence of high methanol concentration. The crude enzyme which maintained 90% of its original activity after being treated at 70°C was purified and the properties were characterized. The partially purified esterase preparation had temperature and pH optima of 60°C and 8.0 respectively. The enzyme retained almost complete activity in presence of 25% methanol and 80% activity in the same strength of ethanol. Conditions of enzyme production were optimized, which lead to 9 fold increase in the esterase yield. One of the isoforms of the enzyme LIP1 was purified to homogeneity and characterized. Purified LIP1 had a K m and V max of 0.01 and 1.12, respectively. The purified esterase lost its thermo and halo tolerance but interestingly, retained 97% activity in methanol.

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“…Due to the surface hydrophobic patches on esterases, ammonium sulfate precipitation followed by HIC can be considered as an effective two-step purification strategy for esterases [21]. …”

Section: Resultsmentioning

confidence: 99%

Esterase Active in Polar Organic Solvents from the YeastPseudozymasp. NII 08165

et al. 2014

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“…RSJ-1 and Pseudomonas sp. AG-8 [29][30][31]. High activity and excellent thermostability at high temperature are useful characteristics for the WCL that would be used in biotransformation fields.…”

Section: Resultsmentioning

confidence: 98%

Production and Characteristics of the Whole-Cell Lipase from Organic Solvent Tolerant Burkholderia sp. ZYB002

Shu

Cheng

et al. 2011

Appl Biochem Biotechnol

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The thermostable and organic solvent tolerant whole-cell lipase (WCL) was produced by Burkholderia sp. ZYB002 with broad spectrum organic solvent tolerance. The production medium of the WCL was primarily optimized, which resulted in the maximum activity of 22.8 U/mL and the 5.1-fold increase of the WCL yield. The optimized culture medium was as follows (% w/v or v/v): soybean meal 2, soybean oil 0.5, manganese sulfate 0.1, K(2)HPO(4) 0.1, olive oil 0.5, initial pH 6.0, inoculum density 2, liquid volume 35 mL in 250-mL Erlenmeyer flask, and incubation time 24 h. The biochemical characterization of the WCL from Burkholderia sp. ZYB002 was determined, and the results showed that the optimal pH and temperature for lipolytic activity of the WCL was 8.0 and 65°C, respectively. The WCL was stable at temperature up to 70°C for 1 h and retained 79.2% of its original activity. The WCL was highly stable in the pH range from 3.0 to 8.5 for 6 h. Ca(2+), K(+), Na(+), NO (3) (-) , etc. ions stimulated its lipolytic activity, whereas Zn(2+) ion caused inhibition effect. The WCL was also relatively stable in n-butanol at a final concentration of 50% (v/v) for 24 h. However, the WCL was strongly inhibited in Triton X-100 at a final concentration of 10% (v/v). The WCL with thermal resistance and organic solvent tolerance showed its great potential in various green industrial chemical processes.

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“…At pH 8, it lost up to 50% activity at the end of a 12 h exposure (Dalal et al, 2008). In another study, Karadzic et al (2006) isolated and purified an extracellular lipase from Pseudomonas aeruginosa.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of two functionally diverse lipases from soil metagenome

Khan

Kottur

Mookambikay

2013

J. Gen. Appl. Microbiol.

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IntroductionLipases are ubiquitous enzymes that catalyze the hydrolysis of fats and oils and form a large group of the enzymes. These enzymes also catalyze the hydrolysis of a wide range of carboxyl esters at the water lipid interface and reverse the reaction in the nonaqueous phase. During the last decade, lipases have gained importance, to a certain extent, over proteases and amylases, especially in food industry. Many lipases have been isolated from bacteria, fungi, plants, and animals, and have received much attention as biocatalysts. The enantioselective and regioselective nature of lipases has been used for the resolution of chiral drugs, fat modification, synthesis of cocoa butter substituent, biofuels, and flavor enhancers. Owing to their novel and multifunctional application, lipase-catalyzed processes have received great attention, mainly due to several advantages: (1) they are more environmentfriendly than bulk chemical syntheses, (2) they allow manufacture of higher quality products, (3) they are easy to recover and re-use and (4) they can be used in continuous operations.Although the microbial diversity in nature has been estimated by culture-independent methods, it is uncertain whether it would be possible to find a universal J. Gen. Appl. Microbiol., 59, 21 31 (2013) A soil metagenomic library was constructed and two functionally diverse lipase genes, SMlipB and SMlipD, were screened by a function-driven approach and characterized. The optimal temperature for enzyme activity of SMlipB and SMlipD was 50°C and 30°C, respectively, and optimal pH was determined to be 7.0 and 9.0, respectively. Both enzymes exhibited broad substrate specificity and showed enhanced activity in the presence of SDS and Tween 20. The SMlipB enzyme was highly resistant to many organic solvents, especially isopropanol, ethanediol, DMSO, methanol and xylene, whereas SMlipD activity was inhibited in all the solvents except xylene.

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Purification and properties of the alkaline lipase from Burkholderia cepacia A.T.C.C. 25609

Cited by 36 publications

References 44 publications

Esterase Active in Polar Organic Solvents from the YeastPseudozymasp. NII 08165

Esterase Active in Polar Organic Solvents from the YeastPseudozymasp. NII 08165

Production and Characteristics of the Whole-Cell Lipase from Organic Solvent Tolerant Burkholderia sp. ZYB002

Cloning and characterization of two functionally diverse lipases from soil metagenome

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