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Immobilization of Pseudomonas cepacia lipase in a phyllosilicate sol–gel matrix: effectiveness as a biocatalyst
Author(s) -
Hsu AnFei,
Foglia Thomas A.,
Shen Siyan
Publication year - 2000
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba19990090
Subject(s) - lipase , chemistry , hydrolysis , lauric acid , pseudomonas , chromatography , triacylglycerol lipase , immobilized enzyme , matrix (chemical analysis) , biocatalysis , orthosilicate , organic chemistry , tetraethyl orthosilicate , catalysis , enzyme , bacteria , fatty acid , biology , genetics , ionic liquid
A novel procedure is described for immobilizing a lipase from Pseudomonas cepacia (PS‐30) within a phyllosilicate sol–gel matrix. The method is based on cross‐linking a phyllosilicate clay with silicate polymers produced by the controlled hydrolysis of tetramethyl orthosilicate (TMOS). The activity of the phyllosilicate sol–gel‐immobilized lipase was dependent upon the type of alkylammonium salt, inorganic catalyst and volume ratio of phyllosilicate clay to TMOS used. Lipase PS‐30 immobilized in this way was more stable and had higher activity compared with the free lipase. Studies on the lipase‐catalysed esterification of lauric acid with octan‐1‐ol in iso‐octane showed that under controlled water activity conditions the phyllosilicate sol–gel‐immobilized lipase had better activity compared with other supported lipase preparations. In addition, the phyllosilicate sol–gel‐immobilized lipase was reusable for at least five esterification cycles without significant loss of activity.