Article

고압에서 β-glucosidase 반응속도론 및 평형에 관한 연구

한진영1, 이승주1,*
Jin Young Han1, Seung Ju Lee1,*
Author Information & Copyright
1동국대학교 식품생명공학과
1Department of Food Science and Biotechnology, Dongguk University
*Corresponding author: Seung Ju Lee, Department of Food Science and Biotechnology, Dongguk University, Seoul, 100-715, Korea, Tel: +82-2-2260-3372; Fax: +82-2-2260-3372, E-mail: Lseungju@dongguk.edu

ⓒ Copyright 2011 Korean Society for Food Engineering. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Apr 05, 2011; Revised: Jul 19, 2011; Accepted: Jul 21, 2011

Published Online: Aug 31, 2011

Abatract

β-Glucosidase enzyme reaction under high hydrostatic pressure was investigated in terms of physical chemistry. A model substrate (p-nitrophenyl-β-D-glucopyranoside (pNPG)) was used, and the pressure effects on the enzymatic hydrolysis (pNPG→pNP) at 25 MPa, 50 MPa, 75 MPa, and 100 MPa were analyzed. Two parts of the reaction such as kinetic and equilibrium stages were considered for mathematical modelling, and their physicochemical parameters such as forward and inverse reaction constants, equilibrium constant, volume change by pressure, etc. were mathematically modeled. The product concentration increased with pressure, and the two stages of reaction were observed. Prediction models were derived to numerically compute the product concentrations according to reaction time over kinetic to equilibrium stages under high pressure condition. Conclusively, the β-glucosidase enzyme reaction could be activated by pressurization within 100 MPa, and the developed models were very successful in their prediction.

Keywords: high hydrostatic pressure; enzyme reaction; equilibrium constant; kinetics; β-glucosidase