Catalytic properties of lipases immobilized on various mesoporous silicates.
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.
Kato
Katsuya
K
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
Irimescu
Roxana
R
Saito
Takao
T
Yokogawa
Yoshiyuki
Y
Takahashi
Haruo
H
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
D004800:Enzymes, Immobilized; D017640:Silicates; D012997:Solvents; D008049:Lipase