Regulation of catalytic activity of acid phosphatase by lipids in a reverse micellar system

Abstract

The influence of biomembrane lipids on the catalytic activity of a peripheral membrane enzyme, acid phosphatase (AP), was studied in a reverse micellar system. It was found that the interaction of AP with lipids led to a number of kinetic effects depending on lipid nature on enzyme function. The observed effects might be caused by the formation of lipoprotein complexes as well as by the influence of lipids on structure and properties of the micellar matrix. The results are important for clear understanding of molecular mechanisms of regulation of the catalytic activity of the membrane-associated enzyme in vivo. These data can also be used as a physicochemical basis for application of AP in medical fields as a diagnostic tool for diseases caused by changes in lipid metabolism, e.g. urinary, orthopedic, and allergic diseases.

Regulation of acid phosphatase in reverse micellar system by lipids additives: Structural aspects

“…Indeed, some proteins have specific binding domains for inositol lipids, which might regulate their activity [35][36][37][38]. In the case of AP, the formation of such complex in aqueous solution was recently confirmed [27]. The result of complex formation between AP and PI can be an increase in the effective protein size and, respectively, the shift of the enzyme activity profile towards higher hydration degrees.…”

“…Thereby the surfactant shell works like a molecular matrix, re-adjusting and supporting the native protein conformation. In the case of enzymes existing in different oligomeric forms, the activity profile shows several optima, and each of them corresponds to specific oligomeric form of enzyme [15,[25][26][27][28][29].…”

Preparative purification of bromelain (EC 3.4.22.33) from pineapple fruit by high-speed counter-current chromatography using a reverse-micelle solvent system

“…In the present study, several surfactants, such as AOT, CTAB and TOMAC, and several chemicals, including sodium phosphate, KCl, isooctane, hexylalcohol and water, were used to prepare the reverse micelle phases according to the literature Kudryashova et al (2009). The forward extraction ratio and back extraction ratio of the crude protein in each reverse micelle solvent system were detected by UV spectra at 280 nm.…”

“…There are some advantages in using the reverse micelle solvent system for protein separation, such as large-scale sample loading, simple operation and continuous preparation (Dong, Meng, Feng, & Sun, 2010;Kudryashova, Bronza, & Levashov, 2009). Thus, the reverse micelle solvent system is a very attractive system, and it has been widely used in protein separation and enrichment (Anarbaev, Rogozina, & Lavrik, 2009Osakai & Shinohara, 2008.…”

Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface

“…[29][30][31][32] Enzymatic activity of AP in AOT RMs formed with conventional organic solvents (aliphatic and aromatic) has been reported. [33][34][35][36] The effects of water content, temperature, external solvent, and surfactant concentration on enzyme activity were evaluated. 37 However, even though the pH value is one of the most relevant parameters for this enzyme, it has not been studied in detail in micellar systems formed by biocompatible solvents.…”