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Hydrolysis of butteroil by immobilized lipase using a hollow‐fiber reactor: Part I. Lipase adsorption studies
Author(s) -
Malcata F. Xavier,
Garcia Hugo S.,
Hill Charles G.,
Amundson Clyde H.
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.260390609
Subject(s) - lipase , adsorption , chemistry , microporous material , langmuir , chromatography , hydrolysis , membrane , aspergillus niger , chemical engineering , triacylglycerol lipase , organic chemistry , enzyme , biochemistry , engineering
Adsorption of proteins from a crude preparation containing a lipase from Aspergillus niger on microporous polypropylene hollow fibers was studied at six different temperatures. Langmuir isotherms accurately describe the overall adsorption equilibria. Lipase is selectively adsorbed relative to the other proteins in the crude preparation. Hence, immobilization also provides further purification of the lipase. The predictions of the Langmuir model for the change in the specific activity of lipase upon adsorption are consistent with experimental results. The loading capacity of the hollow fibers decreases and the adsorption constant increases as temperature is increased. This effect is more significant in the case of lipolytic activity than it is for the total amount of adsorbed protein. Small, positive enthalpy changes are associated with the adsorption of lipase on these hydrophobic membranes.