Article

차가버섯 용매추출분획의 Acetylcholinesterase 저해활성에 대한 동역학 및 열역학적 해석

김학규1, 허원2, 홍억기2, 이신영2,*
Hak-Kyu Kim1, Won Hur2, Eock Kee Hong2, Shin-Young Lee2,*
Author Information & Copyright
1(사)한국가속기 및 플라스마연구협회
2강원대학교 생물공학과
1Korea Accelerator and Plasma Research Association
2Department of Bioengineering and Technology, Kangwon National University
*Corresponding author: Shin-Young Lee, Department of Bioengineering and Technology, Kangwon National University, Chuncheon, 200-701, Korea, Tel: +82-33-250-6273, Fax: +82-33-243-6350, E-mail: sylee@kangwon.ac.kr

ⓒ 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: May 30, 2011; Revised: Sep 02, 2011; Accepted: Sep 08, 2011

Published Online: Nov 30, 2011

Abatract

Twenty four fractions by solvent extraction and/or acid precipitation from fruit body and culture broth of Inonotus obliquus were prepared, and their inhibitory effect against acetylcholinesterase (AChE) was investigated. Among these fractions, acid (1 M HCl) precipitates from cell-free culture broth and fruit body exhibited the highest inhibitory effect on AChE in vitro. Acid precipitates inhibited AChE activity in a concentration-dependant manner and IC50 values of both acid precipitates were 0.53 mg/mL. The inhibition pattern was general non-competitive inhibition. The energetic parameters were also determined by dual substrate/temperature design. Both acid precipitates increased the values of Ea, ΔH, ΔG and ΔH* decreasing the value of ΔS for AChE. The results implied that the acid precipitates from I. obliquus increased the thermodynamic barrier, leading to the breakdown of ES complex and the formation of products as inhibitory mechanism.

Keywords: Inonotus obliquus; solvent extract; acid precipitate; acetylcholinesterase; inhibition kinetics and thermodynamic analysis