Characterization and utilization of Candida rugosa lipase immobilized on controlled pore silica

• Published in: Applied biochemistry and biotechnology Vol. 77-79; no. 1-3; pp. 745 - 757
• Main Authors: SOARES, C. M. F, DE CASTRO, H. F, DE MORAES, F. F, ZANIN, G. M
• Format: Conference Proceeding Journal Article
• Language: English
• Published: Heidelberg Springer 1999; Springer Nature B.V
• Subjects: Biochemistry; Biological and medical sciences; Biotechnology; Candida rugosa; Fundamental and applied biological sciences. Psychology; Fungi; Immobilization of enzymes and other molecules; Immobilization techniques; Methods. Procedures. Technologies; Studies; Temperature; Yeast; Support; Enzyme; Immobilization; Triacylglycerol lipase; Esterases; Silica; Esterification; Thermal stability; Carboxylic ester hydrolases; Fungi; Hydrolysis; Enzymatic activity; Hydrolases; Fungi Imperfecti; Immobilized enzyme; Candida rugosa; Thallophyta
• ISSN: 0273-2289; 1559-0291; 0273-2289
• DOI: 10.1385/abab:79:1-3:745

Candida rugosa lipase was immobilized by covalent binding on controlled pore silica (CPS) using glutaraldehyde as cross-linking agent under aqueous and nonaqueous conditions. The immobilized C. rugosa was more active when the coupling procedure was performed in the presence of a nonpolar solvent, hexane. Similar optima pH (7.5-8.0) was found for both free and immobilized lipase. The optimum temperature for the immobilized lipase was about 10 degrees C higher than that for the free lipase. The thermal stability of the CPS lipase was also greater than the original lipase preparation. Studies on the operational stability of CPS lipase revealed good potential for recycling under aqueous (olive-oil hydrolysis) and nonaqueous (butyl butyrate synthesis) conditions.