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Continuous hydrolysis of olive oil by lipase in microporous hydrophobic membrane bioreactor
Author(s) -
Hoq Mohammad Mozammel,
Yamane Tsuneo,
Shimizu Shoichi,
Funada Tadashi,
Ishida Shiro
Publication year - 1985
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/bf02935705
Subject(s) - lipase , chemistry , hydrolysis , chromatography , microporous material , membrane bioreactor , adsorption , membrane , bioreactor , glycerol , triacylglycerol lipase , immobilized enzyme , organic chemistry , biochemistry , enzyme
Continuous hydrolysis of olive oil by Candida cylindracea's lipase was studied in a microporous hydrophobic membrane bioreactor. Olive oil and buffer solution, fed continuously through two compartments partitioned by membrane, caused reaction at the interface of lipase‐adsorbed membrane and buffer solution. Fatty acid was obtained in a single phase without being mixed with components of other phases. At all mean residence times, countercurrent flow mode was superior to cocurrent one. The lipase was adsorbed onto the membrane, and its adsorption was suggested to be partially specific from the experiments with enzymes having various levels of purity. The percent hydrolysis depended hyperbolically on the interfacial enzyme concentration. The hydrolysis seemed to be limited by diffusion of fat or fatty acid through the micropores of the membrane at higher interfacial enzyme concentrations. The lipase was stabilized significantly by glycerol added to the buffer solution. Satisfactory performance of the membrane bioreactor was obtained in a longterm continuous operation which lasted for 24 days by feeding buffer‐glycerol (18.0%) solution over the adsorbed lipase. The operational half‐life of the adsorbed enzyme was 15 days at 40 C.