Enzymatic activity of alkaline phosphatase adsorbed on dimyristoylphosphatidic acid Langmuir-Blodgett films

被引：46

作者：

Caseli, L ^{[1
]}

Zaniquelli, MED ^{[1
]}

Furriel, RPM ^{[1
]}

Leone, FA ^{[1
]}

机构：

[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, BR-14040901 Ribeirao Preto, SP, Brazil

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2002年 / 25卷 / 02期

基金：

巴西圣保罗研究基金会;

关键词：

alkaline phosphatase; dimyristoyl phosphatidic acid; Langmuir monolayers; enzymatic catalysis; adsorption isotherm; non-ionic surfactant;

D O I：

10.1016/S0927-7765(01)00302-2

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The kinetics and the adsorption isotherms of the surfactant-solubilized alkaline phosphatase from rat osseous plate adsorbed by dip-coating on dimyristoyl phosphatidic acid (DMPA) Langmuir-Blodgett (LB) films were studied. The phosphomonohydrolase activity of the enzyme on the LB film was estimated by the hydrolysis of p-nitrophenylphosphate (PNPP). Films prepared from solutions containing 0.30 mug ml(-1) of protein showed maximum activity for the supported enzyme above the critical micellar concentration of the non-ionic surfactant (polyoxyethylene-9-lauryl ether) used for enzyme solubilization. The surface density of the enzyme on DMPA LB films was determined from quartz crystal microbalance measurements. A consistent explanation concerning the maximum enzymatic activity is supported by data of surface tension for the mixed non-ionic surfactant -enzyme system. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：119 / 128

页数：10

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