z-logo
Premium
Gas phase transesterification reactions catalyzed by lipolytic enzymes
Author(s) -
Parvaresh Firooze,
Robert Hervé,
Thomas Daniel,
Legoy MarieDominique
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260390415
Subject(s) - cutinase , transesterification , propionate , chemistry , lipase , organic chemistry , catalysis , enzyme , propionates , chromatography
Porcine pancreatic lipase and Fusarium solani cutinase were used to catalyze transesterification reactions between methyl propionate, ethyl propionate, and a series of primary alcohols at high temperatures in a continuous packed‐bed gas‐solid reactor, in which the solid phase is composed of the enzyme and the substrates and products are in a gaseous form. In this type of system, enzyme activity was found to depend essentially on the water activity ( A w ) of the enzyme preparation.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom