title: Catalytic properties of lipases immobilized on various mesoporous silicates.
abstract: Lipases SP525, AK, LIP, and PS were immobilized on three kinds of mesoporous silicates (FMS, PESO, and SBA) with diameters of 27 to 92 A. The amount of lipase activity adsorbed on these supports was related to the pore size of the silicate. Enantioselectivities of immobilized lipases were similar to those of free lipases, and recycling could be done in both aqueous and organic solvents.
authors.affiliation: Bio-functional Ceramics Group, Ceramics Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 2266-98 Anagahora, Shimoshidami, Moriyama-ku, Nagoya 463-8560, Japan. katsuya-kato@aist.go.jp
authors.forename: Katsuya
authors.initials: K
authors.lastname: Kato
authors.forename: Roxana
authors.initials: R
authors.lastname: Irimescu
authors.forename: Takao
authors.initials: T
authors.lastname: Saito
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Yokogawa
authors.forename: Haruo
authors.initials: H
authors.lastname: Takahashi
mesh_terms: D000107:Acetylation; D000327:Adsorption; D002384:Catalysis; D004355:Drug Stability; D004800:Enzymes, Immobilized; D006358:Hot Temperature; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification; D016062:Porosity; D017640:Silicates; D012997:Solvents; D013237:Stereoisomerism; D013816:Thermodynamics
chemical_list: D004800:Enzymes, Immobilized; D017640:Silicates; D012997:Solvents; D008049:Lipase