Esterase activity of biocomposites constituted by lipases adsorbed on layered zirconium phosphate and phosphonates: selective adsorption of different enzyme isoforms

被引:29
作者
Bellezza, F
Cipiciani, A
Costantino, U
机构
[1] Univ Perugia, Dipartimento Chim, Chim Organ Lab, I-06123 Perugia, Italy
[2] Univ Perugia, Dipartimento Chim, Lab Chim Inorgan, I-06123 Perugia, Italy
关键词
lipase; enzyme immobilization; zirconium phosphates; zirconium phosphonates; adsorption;
D O I
10.1016/S1381-1177(03)00164-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Aqueous solutions of crude extract of lipase from Candida rugosa (C-CRL) and of a semipurified material obtained by treating C-CRL with propan-2-ol (PT-CRL) were used as a source of biomaterial for its adsorption onto the surface of layered micro-crystals of (alpha-zirconium phosphate Zr(HPO4)(2) and phosphonates such as Zr(C6H5PO3)(2), Zr(HPO4)(C6H5PO3) and Zr(HOOCCH PO3)(HPO4), which possess groups with different hydrophobic character anchored to the inorganic matrix. Several biocomposites have been obtained by changing the temperature and the time of equilibration of the various supports with the C-CPL and PT-CRL solutions. The biocomposites have shown different esterase activities and enantio-selectivities in the hydrolysis of p-nitrophenylacetate (p-NPA), ethyl butyrate and (+/-)-methyl-2-(4-chlorophenoxy) propionate as a function of the nature of the support and of the time and temperature of equilibration. These results have been interpreted on the basis of a selective adsorption of different isoforms of the enzyme. The biocomposites can be stored for more than 1 month at 4degreesC and can be used for several cycles without a significant decrease in catalytic activity. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:47 / 56
页数:10
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