4.6 Article

Effect of immobilization on thermostability of lipase from Candida rugosa

Journal

BIOCHEMICAL ENGINEERING JOURNAL
Volume 14, Issue 1, Pages 75-77

Publisher

ELSEVIER SCIENCE SA
DOI: 10.1016/S1369-703X(02)00138-9

Keywords

thermostability; lipase; immobilized enzyme

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Immobilized lipases are becoming increasingly useful for biotechnological processing. In this study, the thermostability of immobilized lipases from Candida rugosa is investigated. Lipase is immobilized in calcium alginate gel, in inorganic microcapsules of calcium silicate, and on macroporous acrylic beads. The thermostability of lipase is found to be enhanced according to the type of immobilization used. In particular, lipase immobilized in alginate gels incubated below 60 degreesC shows a higher stability than free or other immobilized lipases. This is due to the strong affinity between lipase and alginate. Likewise, lipase incubated above 60 degreesC is stabilized for the lipase immobilized in inorganic microcapsules. This is due to the stabilization of the lipase's intermediate state. (C) 2002 Elsevier Science B.V. All rights reserved.

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