Esterification of lauric acid using lipase immobilized in the micropores of a hollow‐fiber membrane

• Published in: Journal of the American Oil Chemists' Society Vol. 83; no. 3; pp. 209 - 213
• Main Authors: Goto, Muneharu, Kawakita, Hidetaka, Uezu, Kazuya, Tsuneda, Satoshi, Saito, Kyoichi, Goto, Masahiro, Tamada, Masao, Sugo, Takanobu
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer‐Verlag 01.03.2006; Springer; Springer Nature B.V
• Subjects: Acids; Biological and medical sciences; Chemistry; Enzymatic esterification; Enzymes; Fat industries; Food industries; Fundamental and applied biological sciences. Psychology; graft polymerization; hollow‐fiber; immobilization; lauric acid; lipase; Membranes; Oils & fats; polymer brush; Polymerization; Polymers; Rhizopus sp; hollow-fiber; Enzyme; Rhizopus sp; lipase; Immobilization; Polymerization; Triacylglycerol lipase; Polymer; polymer brush; Esterases; Enzymatic esterification; Esterification; Carboxylic ester hydrolases; Oils and fats industry; Hydrolases; lauric acid; graft polymerization; Enzymatic reaction
• ISSN: 0003-021X; 1558-9331
• DOI: 10.1007/s11746-006-1195-x

A porous anion‐exchange hollow‐fiber membrane was prepared by radiation‐induced graft polymerization and chemical modification to immobilize lipase for enzymatic reaction in an organic solvent. The amount of anion‐exchange group introduced to the porous hollow‐fiber membrane was 2.5 mol/kgfiber. A lipase solution was allowed to permeate through the porous anion‐exchange hollow‐fiber membrane, and lipase molecules that adsorbed onto the grafted polymer brush were cross‐linked with glutaraldehyde. The lipase was immobilized at a density of 0.14 kglipase/kgfiber, which was equivalent to a degree of multilayer binding of 20. Esterification was carried out by passing a solution of lauric acid and benzyl alcohol in anhydrous issoctane through the lipase‐immobilized membrane, and lipase activity was determined. A reaction percentage of 50% was achieved at space velocity 68 h−1. The maximum immobilized lipase and native lipase activities were 8.9 and 0.38 mol/(h·kglipase), respectively. Thus, the activity of the immobilized lipase was 23.4 times higher than that of the native lipase.