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Repeated use of immobilized lipase for monoacylglycerol production by solid‐phase glycerolysis of olive oil
Author(s) -
Rosu Roxana,
Uozaki Yuki,
Iwasaki Yugo,
Yamane Tsuneo
Publication year - 1997
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/s11746-997-0104-2
Subject(s) - monoacylglycerol lipase , lipase , chemistry , olive oil , chromatography , immobilized enzyme , adsorption , catalysis , pseudomonas , biopolymer , enzyme , organic chemistry , food science , biochemistry , bacteria , biology , polymer , endocannabinoid system , receptor , genetics
By using immobilized lipase for production of monoacylglycerol (MAG) by solid‐phase glycerolysis of fats and oils, the enzyme could be recovered easily from the reaction mixture and recycled to reduce the cost of the catalyst. Several support materials (CaCO 3 , CaSO 4 ·2H 2 O, Ca 2 P 2 O 7 , and Celite) were screened for immobilization of Pseudomonas sp. lipase by adsorption and tested for solid‐phase glycerolysis of olive oil. Immobilization made the reuse of enzyme feasible. CaCO 3 proved to be the best support: 90% MAG (wt% in the glycerolfree reaction mixture after 72 h of reaction time) was obtained until the fifth use, 80% after the seventh use, and 60% after the tenth use. The same support was found suitable for immobilization of two other bacterial lipases from Chromobacterium viscosum and Pseudomonas pseudoalkali .