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共溶质对牛血清白蛋白结构形成的热力学效应。

Thermomechanical effects of co-solute on the structure formation of bovine serum albumin.

机构信息

School of Applied Sciences, RMIT University, City Campus, Melbourne, VIC 3001, Australia.

Animal, Food and Health Sciences, CSIRO, Werribee, VIC 3030, Australia.

出版信息

Food Chem. 2014 Aug 15;157:296-301. doi: 10.1016/j.foodchem.2014.02.041. Epub 2014 Feb 22.

DOI:10.1016/j.foodchem.2014.02.041
PMID:24679784
Abstract

The effect of glucose syrup on the structural properties of bovine serum albumin has been addressed in preparations from low to high solids. Fifteen percent protein was mixed with the co-solute at concentrations up to 65% and subjected to thermal treatment to examine the changes in phase and state transitions. Thermomechanics were the working protocol being carried out with micro differential scanning calorimetry and small deformation dynamic oscillation. Results argue that protein molecules have been extensively stabilised by the addition of a co-solute, recorded via a delayed thermal denaturation. Further, increasing the glucose syrup enhanced polymer-polymer interactions leading to stronger networks following thermal denaturation of the globular protein. Condensed BSA/glucose syrup mixtures, i.e. at 80% solids, were cooled at subzero temperatures to exhibit a considerable state of vitrification. Molecular relaxation phenomena were successfully followed using theoretical concepts from synthetic polymer research to yield the mechanical glass transition temperature.

摘要

在低至高固含量的制剂中研究了葡萄糖浆对牛血清白蛋白结构特性的影响。将 15%的蛋白质与共溶剂混合,浓度高达 65%,并进行热处理以检查相态和状态转变的变化。热机械学是通过微差示扫描量热法和小变形动态振荡进行的工作方案。结果表明,通过延迟热变性,添加共溶剂可以极大地稳定蛋白质分子。此外,随着葡萄糖浆的增加,增强了聚合物-聚合物相互作用,从而在球形蛋白质热变性后形成更强的网络。在亚零温度下冷却浓缩的 BSA/葡萄糖浆混合物(即 80%固含量),以表现出相当大的玻璃化状态。使用来自合成聚合物研究的理论概念成功地跟踪了分子弛豫现象,以得出力学玻璃化转变温度。

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