Covalent immobilization of pure lipases A and B from Candida rugosa

Covalent immobilization on agarose and SiO 2 of pure lipase A (LIP.A) and B (LIP.B) from C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords m...

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Veröffentlicht in:Journal of molecular catalysis. B, Enzymatic Enzymatic, 1997-01, Vol.2 (4), p.177-184
Hauptverfasser: Moreno, JoséM, Hernaiz, María J, Sánchez-Montero, JoséM, Sinisterra, JoséV, Bustos, M.Teresa, Sánchez, M.Eva, Bello, JoséF
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container_end_page 184
container_issue 4
container_start_page 177
container_title Journal of molecular catalysis. B, Enzymatic
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creator Moreno, JoséM
Hernaiz, María J
Sánchez-Montero, JoséM
Sinisterra, JoséV
Bustos, M.Teresa
Sánchez, M.Eva
Bello, JoséF
description Covalent immobilization on agarose and SiO 2 of pure lipase A (LIP.A) and B (LIP.B) from C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords more stable biocatalysts than on SiO 2. Kinetic studies of all these lipases and derivatives in the hydrolysis of ( R)-(+) and ( S)-(−) methyl 2-chloropropionates were performed and their enantiomeric ratios ( E = ( V max K m ) fast ( V max K m ) slow ) calculated. The results show that (i) purification of the commercial lipase increased the E value 2.5-fold; (ii) both isoenzymes have similar E values, and (iii) in general, the E value increases with the immobilization process.
doi_str_mv 10.1016/S1381-1177(96)00029-X
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subjects Biological and medical sciences
Biotechnology
Candida rugosa
Fundamental and applied biological sciences. Psychology
Immobilization
Immobilization of enzymes and other molecules
Immobilization techniques
Lipases
Methods. Procedures. Technologies
title Covalent immobilization of pure lipases A and B from Candida rugosa
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