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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.