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Enzyme hydrolysis of babassu oil in a membrane bioreactor
Author(s) -
bio Mer on F,
Sant Anna Geraldo Lippel,
Nobrega Ronaldo
Publication year - 2000
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/s11746-000-0165-7
Subject(s) - lipase , membrane , chromatography , hydrolysis , chemistry , membrane bioreactor , bioreactor , immobilized enzyme , triacylglycerol lipase , adsorption , cellulose , membrane reactor , enzyme , organic chemistry , biochemistry
This work deals with the enzymatic hydrolysis of babassu oil by immobilized lipase in a membrane bioreactor using unmixed aqueous and lipid streams. The experimental work was carried out in a flat plate membrane module with two different membranes: hydrophobic (nylon) and hydrophilic [mixed cellulose esters (MCE)], with different nominal pore sizes ranging from 0.10 to 0.65 μm. Candida cylindracea lipase was adsorbed on the membrane surface area, and the reactor was operated in batch mode. The initial enzymatic rate increased from 80 to 150 μmol H + /min when the organic phase velocity increased from 1.0×10 −3 to 3.0×10 −3 m/s, indicating that mass transfer in that phase was the process‐limiting step. Calcium ions had a marked effect on immobilized lipase activity, increasing around twofold the lipolytic activity. Long‐term experimental runs showed that the immobilized lipase remained stable for at least 8 d. The values for immobilized protein and maximal productivities observed for 0.45 μm membranes were: 1.01 g/m 2 and 193 μmol H + /m 2 ·s for MCE membrane and 0.78 g/m 2 and 220 μmol H + /m 2 ·s for nylon membrane. The productivities obtained are among the highest values reported in the technical literature.