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Biotechnology and Applied Biochemistry (2002) 36, (7–12) (Printed in Great Britain)

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Immobilization, stability and esterification studies of a lipase from a Bacillus sp.

Nirpjit S. Dosanjh and Jagdeep Kaur¹

Department of Biotechnology, Panjab University, Chandigarh 160014, India

Key words: enzymic reaction, ester synthesis, half-life, thermostability.

Abbreviations used: CS, CNBr-activated Sepharose 4B; PS, phenyl-Sepharose.

¹Present address and address for correspondence: Department of Pharmacology, School of Medicine, BRB II/III, 8th Floor, Room No. 833, 421 Curie Blvd., Philadelphia, PA 19104-6160, U.S.A. (e-mail jagsekhon@yahoo.com).

In the present paper a comparative account of the immobilization of a Bacillus lipase on different solid supports with different surface properties and their thermostability is presented. Immobilization enhanced the thermostability of lipase. At higher temperatures, lipase immobilized and cross-linked on a hydrophobic surface showed the maximum thermostability. The optimum temperature for immobilized lipase was 9 °C higher than for the free enzyme, while the pH optima were the same. The half-life of soluble lipase at 50 °C was calculated to be 4.5 h, while immobilized lipase did not lose any activity even after 8 h. The temperature stability (for 1 h) of immobilized enzyme was enhanced from 50 to 60 °C in comparison with non-immobilized enzyme. Applications of immobilized lipase for esterification are also presented.

Received 28 August 2001/29 January 2002; accepted 9 April 2002

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