The equilibrium position in lipase mediated esterification of various fatty acids and butanol was studied. The influence of the chain length and the presence of unsaturations in the fatty acids on the equilibrium position was measured and predicted. To predict equilibrium position the program TREP e
Influence of the nature of modifier in the enzymatic activity of chemical modified semipurified lipase from Candida rugosa
✍ Scribed by M. J. Hernáiz; J. M. Sánchez-Montero; J. V. Sinisterra
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 196 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
Semipurified lipase of Candida rugosa (CRSL) was subjected to chemical modification, and the activities of the modified lipase, in hydrolysis and esterification reactions, were examined. The esterification reactions were carried out in the absence and presence of isooctane. When the enzyme was modified with polyethylene glycol (PEG), two methodologies were studied. The activation of PEG with p-NO 2 -phenylchloroformate gives better biocatalysts than those obtained with cyanuric chloride-PEG. The chemical modification with PEG increases the stability of pure lipases in isooctane at 50°C (extreme conditions). The chemically modified enzymes are useful for biotransformations in organic solvents. In addition the nitration of tyrosines with tetranitromethane was also studied.
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