Openly accessible

Synthesis of ethyl acetate employing celite-immobilized lipase of Bacillus cereus MTCC 8372

Verma, M. L., Azmi, W. and Kanwar, S. S. 2009, Synthesis of ethyl acetate employing celite-immobilized lipase of Bacillus cereus MTCC 8372, Acta microbiologica et immunologica Hungarica, vol. 56, no. 3, pp. 229-242.

Attached Files
Name Description MIMEType Size Downloads
verma-synthesisof-2009.pdf Published version application/pdf 98.43KB 12

Title Synthesis of ethyl acetate employing celite-immobilized lipase of Bacillus cereus MTCC 8372
Formatted title Synthesis of ethyl acetate employing celite-immobilized lipase of Bacillus cereus MTCC 8372
Author(s) Verma, M. L.
Azmi, W.
Kanwar, S. S.
Journal name Acta microbiologica et immunologica Hungarica
Volume number 56
Issue number 3
Start page 229
End page 242
Total pages 14
Publisher Akadémiai Kiadó
Place of publication Budapest, Hungary
Publication date 2009
ISSN 1217-8950
1588-2640
Keyword(s) Bacillus cereus MTCC 8372
celite
immobilization
lipase
transesterification and ethyl acetate synthesis
Summary A wide range of fatty acid esters can be synthesized by esterification and transesterification reactions catalyzed by lipases in non-aqueous systems. In the present study, immobilization of a purified alkaline extra-cellular lipase of Bacillus cereus MTCC 8372 by adsorption on diatomaceous earth (celite) for synthesis of ethyl acetate via transesterification route was investigated. B. cereus lipase was deposited on celite (77% protein binding efficiency) by direct binding from aqueous solution. Immobilized lipase was used to synthesis of ethyl acetate from vinyl acetate and ethanol in n -nonane. Various reaction conditions, such as biocatalyst concentration, substrates concentration, choices of solvents ( n -alkanes), incubation time, temperature, molecular sieves (3Å × 1.5 mm), and water activity(a w ), were optimized. The immobilized lipase (25 mg/ml) was used to perform transesterification in n -alkane(s) that resulted in approximately 73.7 mM of ethyl acetate at 55 °C in n -nonane under shaking (160 rpm) after 15 h, when vinyl acetate and ethanol were used in a equimolar ratio (100 mM each). Addition of molecular sieves (3Å × 1.5 mm) as well as effect of water activity of saturated salt solutions (KI, KCl and KNO 3 ) to the transesterification efficiency has inhibitory effect. Batch operational stability tests indicated that immobilized lipase had retained 50% of its original catalytic activity after four consecutive batches of 15 h each.
Language eng
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 ©2009, Akadémiai Kiadó
Persistent URL http://hdl.handle.net/10536/DRO/DU:30047724

Document type: Journal Article
Collections: School of Life and Environmental Sciences
Open Access Collection
Connect to link resolver
 
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
Citation counts: TR Web of Science Citation Count  Cited 6 times in TR Web of Science
Scopus Citation Count Cited 7 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 56 Abstract Views, 12 File Downloads  -  Detailed Statistics
Created: Mon, 03 Sep 2012, 13:46:56 EST

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.