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http://krishi.icar.gov.in/jspui/handle/123456789/42426
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chakraborty,Kajal | en_US |
dc.contributor.author | Paulraj,R | en_US |
dc.date.accessioned | 2020-11-19T06:00:06Z | - |
dc.date.available | 2020-11-19T06:00:06Z | - |
dc.date.issued | 2010-01-01 | - |
dc.identifier.citation | Not Available | en_US |
dc.identifier.issn | Not Available | - |
dc.identifier.uri | http://krishi.icar.gov.in/jspui/handle/123456789/42426 | - |
dc.description | Not Available | en_US |
dc.description.abstract | An extra-cellular lipase produced by Bacillus licheniformis MTCC 6824 was purified to homogeneity by ammonium sulphate fractionation, ethanol/ether precipitation, dialysis, followed by anion-exchange chromatography on Amberlite IRA 410 (Cl− form) and gel exclusion chromatography on Sephadex G 100 using Tris–HCl buffer (pH 8.0). The crude lipase extract had an activity of 41.7 LU/ml of culture medium when the bacterium was cultured for 48 h at 37 °C and pH 8.0 with nutrient broth supplemented with sardine oil as carbon source. The enzyme was purified 208-fold with 8.36% recovery and a specific activity of 520 LU/mg after gel exclusion chromatography. The pure enzyme is a monomeric protein and has an apparent molecular mass of 74.8 kDa. The lipase had a Vmax and Km of 0.64 mM/mg/min and 29 mM, respectively, with 4-nitro phenylpalmitate as a substrate, as calculated from the Lineweaver–Burk plot. The lipase exhibited optimum activity at 45 °C and pH 8.0, respectively. The enzyme had half-lives (T1/2) of 82 min at 45 °C, and 48 min at 55 °C. The catalytic activity was enhanced by Ca2+ (18%) and Mg2+ (12%) at 30 mM. The lipase was inhibited by Co2+, Cu2+, Zn2+, Fe2 even at low concentration (10 mM). EDTA, at 70 mM concentration, significantly inhibited the activity of lipase. Phenyl methyl sulfonyl fluoride (PMSF, 70 mM) completely inactivated the original lipase. A combination of Ca2+ and sorbitol induced a synergistic effect on the activity of lipase with a significantly high residual activity (100%), even after 45 min, as compared to 91.5% when incubated with Ca2+ alone. The lipase was found to be hydrolytically resistant toward triacylglycerols with more double bonds. | en_US |
dc.description.sponsorship | Not Available | en_US |
dc.language.iso | English | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartofseries | Not Available | - |
dc.subject | Alkaline lipase | en_US |
dc.subject | Bacillus licheniformis MTCC 6824 | en_US |
dc.subject | Anion exchange chromatography | en_US |
dc.subject | Sephadex G 100 gel exclusion chromatography | en_US |
dc.title | Extra-cellular alkaline metallolipase from Bacillus licheniformisMTCC 6824: Purification and biochemical characterization | en_US |
dc.title.alternative | Not Available | en_US |
dc.type | Article | en_US |
dc.publication.projectcode | Not Available | en_US |
dc.publication.journalname | Food Chemistry | en_US |
dc.publication.volumeno | 120 | en_US |
dc.publication.pagenumber | 433-442 | en_US |
dc.publication.divisionUnit | Not Available | en_US |
dc.publication.sourceUrl | http://dx.doi.org/10.1016/j.foodchem.2009.10.032 | en_US |
dc.publication.sourceUrl | http://eprints.cmfri.org.in/4/1/kajal.pdf | en_US |
dc.publication.authorAffiliation | Not Available | en_US |
dc.ICARdataUseLicence | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf | en_US |
dc.publication.naasrating | 12.31 | en_US |
Appears in Collections: | FS-CMFRI-Publication |
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