Immobilization of lipase on a new inorganic ceramics support, toyonite, and the reactivity and enantioselectivity of the immobilized lipase

Citation
M. Kamori et al., Immobilization of lipase on a new inorganic ceramics support, toyonite, and the reactivity and enantioselectivity of the immobilized lipase, J MOL CAT B, 9(4-6), 2000, pp. 269-274
Citations number
15
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
9
Issue
4-6
Year of publication
2000
Pages
269 - 274
Database
ISI
SICI code
1381-1177(20000421)9:4-6<269:IOLOAN>2.0.ZU;2-D
Abstract
A porous ceramics support, Toyonite 200-M (TN-M), for the immobilization of lipases was prepared hydrothermally from the minerals of kaolinite. Compar ed with some other commercial solid supports, the TN-M one exhibited better stability and higher selectivity for lipase proteins, and lipase PS (Pseud omonas cepacia) immobilized on the ceramics support showed higher reactivit y for organic substrates than the free crude enzyme. (C) 2000 Elsevier Scie nce B.V. All rights reserved.