Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles
- 1 July 1993
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 42 (3) , 326-332
- https://doi.org/10.1002/bit.260420309
Abstract
Fusarium solani pisi recombinant cutinase, solubilized in AOT/isooctane‐reversed micelles, was used to catalyze the esterification of fatty acids with aliphatic alcohols. Some relevant parameters for the enzyme activity such as pH, Wo (water/surfactant molar ratio), temperature, and substrate concentration were optimized. Maximal specific activity was obtained for hexanol. The cutinase showed selectivity for short‐chain fatty acids. The stability of the microencapsulated cutinase was investigated at various concentrations of water and different values of pH. Oleic acid had a negative effect on the cutinase stability, while hexanol proved to be a strong stabilizer increasing the half‐life of the enzyme about 45 times. © 1993 John Wiley & Sons, Inc.Keywords
This publication has 15 references indexed in Scilit:
- Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solventNature, 1992
- Gas phase transesterification reactions catalyzed by lipolytic enzymesBiotechnology & Bioengineering, 1992
- Kinetics and stability of a chromobacterium viscosum lipase in reversed micellar and aqueous mediaJournal of Chemical Technology & Biotechnology, 1992
- Characteristics of Lipase Catalysis During Ester Synthesis in Reversed Micellar SystemsBiocatalysis, 1991
- Esterification of Short Chain Organic Acids with Alcohols by a Lipase Microencapsulated in Reversed MicellesBiocatalysis, 1991
- Esterification reactions of lipase in reverse micellesBiotechnology & Bioengineering, 1990
- Lipase-Catalyzed Synthesis of Fatty Acid Esters Useful in the Food IndustryBiocatalysis, 1990
- Reverse micelles as hosts for proteins and small moleculesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1988
- Micellar solubilization of biopolymers in organic solvents. 5. Activity and conformation of .alpha.-chymotrypsin in isooctane-AOT reverse micellesJournal of the American Chemical Society, 1981
- Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisiBiochemistry, 1975