35.5kDa亚基缺失对花生球蛋白受热行为影响

Effect of 35.5 kDa subunit lacking on heating behavior of arachin

以35.5 kDa亚基缺失为研究点,对比了亚基缺失和未缺失花生球蛋白相对分子质量分布、热稳定性、加热聚集性和流体回转半径,明确了35.5 kDa亚基缺失对花生球蛋白受热行为影响。结果表明:35.5 kDa亚基缺失导致花生球蛋白存在形式不同;亚基缺失造成花生球蛋白热稳定性变性协同性增强;亚基缺失和未缺失花生球蛋白在60℃热处理可形成可溶性聚集体,90℃和120℃则形成共价聚集;加热会导致花生球蛋白分子结构松散,松散程度亚基缺失花生球蛋白大于未缺失花生球蛋白。该研究将为筛选适宜热加工花生蛋白提供依据,并为热单元中定向调控提供一定指导。

The relative molecular weight distribution, thermal stability, heat - induced aggregation and radius of gyration of 35.5 kDa subunit lacking arachin were compared with those of normal arachin to study the effect of 35.5 kDa subunit lacking on heating behavior of arachin. The results showed that different molecular species existed in the 35.5 kDa subunit lacking arachin. The lacking of 35.5 kDa subunit could increase thermal stability and denature - cooperativity of arachin. Soluble aggregation formed at 60℃ in subunit lacking and normal arachin, while covalent aggregation formed at 90℃ and 120℃. Heat treatment could lead to a looseness of arachin molecular structure and that of subunit lacking arachin was much more loosen than that of normal arachin. The study could provide the basis for screening protein which was suit for heating and the guidance for directed regulation in thermal processing.