摘要
综述了基因重组技术在揭示大豆球蛋白和 β -伴球蛋白的结构与功能关系方面的研究进展。通过对 β -伴球蛋白组成亚基 (α ,α′和 β)和α ,α′亚基核心区域的功能性质相比较发现 ,亚基核心区域决定着热稳定性和表面疏水性 ;α ,α′亚基的外延区域决定着蛋白质的溶解度和乳化能力 ,碳水化合物部分抑制热诱导聚集体的形成。对不同方式改性的大豆球蛋白前体 (A1aB1b)的功能性质研究表明 ,影响凝胶和乳化性能的结构因素明显不同 ,蛋白C -末端区域的疏水性影响其乳化能力的高低 ,而游离SH基团的拓扑学结构则与热诱导凝胶的形成有着密切的关系。
Structure-function relationships of glycinin and β-conglycinin revealed by using recombinant systems were reviewed. Mutual comparison of functional properties of β-conglycinin constituent subunits (α, α′ and β) and the core regions of α and α′ indicate that the core regions determine thermal stability and surface hydrophobicity, that the extension regions of α and α′ contribute to high solubility and emulsifying abilities and that the carbohydrate moieties inhibit the formation of heat-induced aggregates. Examination of functional properties of various modified versions of proglycinin A1aB1b suggests that the hydrophobicity of the C-terminal region is probably important for a high emulsifying ability,that the topology of free SH residues is closely related to the heat-induced gel forming ability and that the structural factors suitable for gelation and emulsification properties are quite different.
出处
《中国油脂》
CAS
CSCD
北大核心
2004年第11期24-28,共5页
China Oils and Fats
