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Immobilization of porcine pancreatic lipase on celite for application in the synthesis of butyl butyrate in a nonaqueous system
Author(s) -
Castro Heizir F.,
Oliveira Pedro C.,
Soares Cleide M. F.,
Zanin Gisella M.
Publication year - 1999
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-999-0062-y
Subject(s) - lipase , chemistry , pancreatic lipase , aqueous solution , solvent , immobilized enzyme , chromatography , organic chemistry , enzyme
For immobilization of lipase, the use of a porous support material is recommended so that suitable amounts of lipase can be spread on a surface area without conformational changes. In this work, porcine pancreatic lipase was deposited on Celite, either by direct binding from aqueous solution or by deposition from aqueous solution by the addition of organic solvent. The influence of the immobilization procedure on the activities of the derivatives has been studied regarding their ability to synthesize butyl butyrate. The reaction rates were compared with the rate of esterification with free lipase. Better properties were displayed when the immobilized lipase form was prepared in an apolar solvent such as hexane. Under suitable reaction conditions, esterification yields as high as 90% were attained. Batch operational stability tests indicated that no enzyme deactivation occurs after 15 consecutive batches of 24 h each.