Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372 Verma, M. L. and Kanwar, S. S. 2010, Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372, Acta microbiologica et immunologica hungarica, vol. 57, no. 3, pp. 191-207, doi: 10.1556/AMicr.57.2010.3.4. Attached Files Name Description MIMEType Size Downloads verma-purificationand-2010.pdf Published version application/pdf 286.74KB 266 Title Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372 Formatted title Purification and characterization of a low molecular mass alkaliphilic lipase of Bacillus cereus MTCC 8372 Author(s) Verma, M. L. Kanwar, S. S. Journal name Acta microbiologica et immunologica hungarica Volume number 57 Issue number 3 Start page 191 End page 207 Total pages 17 Publisher Akadémiai Kiadó Place of publication Budapest, Hungary Publication date 2010-09 ISSN 1217-8950 1588-2640 Keyword(s) Bacillus cereus MTCC 8372 biochemical characterization detergents and PMSF effect of metal-ions low molecular mass lipase purification Summary A low molecular mass alkaliphilic extra-cellular lipase of Bacillus cereus MTCC 8372 was purified 35-fold by hydrophobic interaction (Octyl-Sepharose) chromatography. The purified enzyme was found to be electrophoretically pure by denaturing gel electrophoresis and possessed a molecular mass of approximately 8 kDa. It is a homopentamer of 40 kDa as revealed by native-PAGE. The lipase was optimally active at 55 °C and retained approximately half of its original activity after 40 min incubation at 55 °C. The enzyme was maximally active at pH 8.5. Mg 2+ , Cu 2+ , Ca 2+ , Hg 2+ , Al 3+ and Fe 3+ at 1 mM enhanced hydrolytic activity of the lipase. Interestingly, Hg 2+ ions synergized and Zn 2+ and Co 2+ ions antagonized the lipase activity. Among surfactants, Tween 80 promoted the lipase activity. Phenyl methyl sulfonyl fluoride (PMSF, 15 mM) decreased 98% of original activity of lipase. The lipase was highly specific towards p -nitrophenyl palmitate and showed a V max and K m of 0.70 mmol.mg −1 .min −1 and 32 mM for hydrolysis of p NPP. Language eng DOI 10.1556/AMicr.57.2010.3.4 Field of Research 069999 Biological Sciences not elsewhere classified Socio Economic Objective 860106 Oils and Fats (incl. Margarines) HERDC Research category C1.1 Refereed article in a scholarly journal Copyright notice ©2010, Akadémiai Kiadó Free to Read? Yes Persistent URL http://hdl.handle.net/10536/DRO/DU:30047723 Document type: Journal Article Collections: Faculty of Science, Engineering and Built Environment School of Life and Environmental Sciences Open Access Collection Related Links Link Description Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au. Versions Version Filter Type Mon, 03 Sep 2012, 13:46:52 EST Thu, 20 Sep 2012, 11:09:39 EST Thu, 20 Sep 2012, 14:25:14 EST Mon, 06 May 2013, 14:11:56 EST Thu, 11 Dec 2014, 18:06:13 EST Tue, 06 Sep 2016, 19:39:19 EST Tue, 05 Dec 2017, 12:35:33 EST Fri, 07 Sep 2018, 16:08:45 EST Filtered Full Citation counts:   Cited 9 times in TR Web of Science Cited 12 times in Scopus Search Google Scholar Access Statistics: 209 Abstract Views, 266 File Downloads  -  Detailed Statistics Created: Mon, 03 Sep 2012, 13:46:52 EST