Conformational Stability of Proteins in Colloidal Food Model System

콜로이드 모델 식품에 있어 단백질의 구조적 안정성

To elucidate the conformational stability of proteins in colloidal food system, molecular properties of various proteins such as chemically modified ${\beta}-lactoglobulin$, bovine serum albumin (BSA) structural intermediates, and ${\beta}-casein$ under chaotropic conditions, were examined using circular dichroism, SS bond content, and hydrodynamic radius determination. As refolding time increases, BSA intermediates approach the conformation of native BSA. And succinylation made ${\beta}-lactoglobulin$ have more aperiodic structure by increasing net negative charge. Also, under chaotropic conditions, the conformation of P-casein was affected by hydrophobic interactions. This study clearly indicates that hydrophobic interactions and electrostatic interactions are major contributing factors in conformational stability of proteins.

콜로이드 식품에서의 단백질의 구조적 안정성을 연구하기 위하여 7개의 BSA structural intermediates, succinylated ${\beta}-lactoglobulin$을 만든 후 CD, 이황화물 결합함량, hydrodynamic radius 등을 측정하여 그 구조적 특성을 규명했다. Refolding time이 길수록 BSA intermediates들은 native BSA 구조에 근접하는 것을 나타냈고 succinylation은 ${\beta}-lactoglobulin$의 순 음전하를 변화시켜 보다 aperiodic structure를 갖게하였다. Perchlorate 존재하 ${\beta}-casein$의 구조는 소수성 상호작용에 크게 영향 받는 것으로 나타났다.