Premium
Immobilization of Candida rugosa lipase by sol‐gel entrapment and its application in the hydrolysis of soybean oil
Author(s) -
Noureddini H.,
Gao X.,
Joshi S.
Publication year - 2003
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/s11746-003-0823-9
Subject(s) - candida rugosa , lipase , thermostability , hydrolysis , immobilized enzyme , chemistry , soybean oil , chromatography , enzyme assay , triacylglycerol lipase , enzyme , nuclear chemistry , organic chemistry , biochemistry
Immobilization of lipase AY from Candida rugosa by entrapment within a chemically inert hydrophobic sol‐gel support was studied. The gel‐entrapped lipase was prepared by polycondensation of hydrolyzed tetramethoxysilane and isobutyltrimethoxysilane. Certain modifications were incorporated into the conventional immobilization procedure, including the use of glucose as additive and the application of vacuum during the drying and aging stages. The activity and thermostability of immobilized enzyme were subsequently determined in hydrolyzing soybean oil. Hydrolysis results showed more than 95 mol% of the theoretical yield for the formation of FF after 1 h of reaction at 40°C. The level of FFA was 3.3 times greater than that seen when an immobilized enzyme was prepared by the conventional sol‐gel process. The immobilized enzyme retained most of its hydrolytic activity compared to the free enzyme and kept more than 95% activity after 120 h of incubation at 40°C, whereas the free enzyme lost 67% of its activity after 24 h of incubation and almost all of its activity after 96 h of incubation at 40°C. The immobilized enzyme also proved to be very stable, as it retained more than 90% of the initial activity after 16 one‐hour reactions. Surface characterization studies suggested that the enzyme‐containing sol‐gel particles have amorphous morphology and are void of micro/meso pores.