Properties of an immobilized lipase of Bacillus coagulans BTS-1

Kanwar, S. S. and Srivastava, M. and Chimni, S. S. and Ghazi, I. A. and Kaushal, R. K. and Joshi, G. K. (2004) Properties of an immobilized lipase of Bacillus coagulans BTS-1. Acta Microbiologica et Immunologica Hungarica, 51 (1-2). pp. 57-73. ISSN 1217-8950

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Lipase (EC is a tri-acylglycerol ester hydrolase, catalysing the hydrolysis of tri-, di-, and mono-acylglycerols to glycerol and fatty acids. To study the effect of adsorption of a lipase obtained from Bacillus coagulans BTS-1, its lipase was immobilized on native and activated (alkylated) matrices, i.e. silica and celite. The effect of pH, temperature, detergents, substrates, alcohols, organic solvent etc. on the stability of the immobilized enzyme was evaluated. The gluteraldahyde or formaldehyde (at 1% and 2% concentration, v/v) activated matrix was exposed to the Tris buffered lipase. The enzyme was adsorbed/entrapped more rapidly on to the activated silica than on the activated celite. The immobilized lipase showed optimal activity at 50ºC following one-hour incubation. The lipase was specifically more hydrolytic to the medium C-length ester (p-nitro phenyl caprylate than p-nitro phenyl laurate). The immobilization/entrapment enhanced the stability of the lipase at a relatively higher temperature (50ºC) and also promoted enzyme activity at an acidic pH (pH 5.5). Moreover, the immobilized lipase was quite resistant to the denaturing effect of SDS.

Item Type: Article
Subjects: Q Science / természettudomány > QR Microbiology / mikrobiológia
Depositing User: xFruzsina xPataki
Date Deposited: 11 Sep 2017 18:38
Last Modified: 11 Sep 2017 18:38

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