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醇法大豆浓缩蛋白(SPC)挤压组织化机理(Ⅱ)──蛋白质变性热力学的差示扫描量热分析法
引用本文:陈莹,沈培英,刘复光.醇法大豆浓缩蛋白(SPC)挤压组织化机理(Ⅱ)──蛋白质变性热力学的差示扫描量热分析法[J].食品与发酵工业,1994(6).
作者姓名:陈莹  沈培英  刘复光
作者单位:华东理工大学生化工程系,无锡轻工业学院粮油工程系
摘    要:采用差示扫描量热法分析大豆蛋白的变性热力学性质。在热变性过程中,醇法大豆浓缩蛋白的结构刚性大、次级键断裂程度低。水对蛋白质的热变性具有一定的促进作用。随着蛋白质水分含量的提高,其热变性温度(Tde)降低。根据这些性质,经调整醇法大豆浓缩蛋白的pH值使其热变性焓差(ΔHd)增大,可实现其挤压组织化。所得挤出物的物理性质及其流变特性均有明显改善。

关 键 词:挤压,蛋白质变性,差示扫描量热

Mechanism of Extrusion Texturization of Alcoholic Leached Soy Protein Concentrate(Ⅱ) ──Thermodynamics of Protein Denaturution by Differential Scanning Calorimetry Analysis
Chen Ying.Mechanism of Extrusion Texturization of Alcoholic Leached Soy Protein Concentrate(Ⅱ) ──Thermodynamics of Protein Denaturution by Differential Scanning Calorimetry Analysis[J].Food and Fermentation Industries,1994(6).
Authors:Chen Ying
Abstract:Thermodynamics of protein denaturation were studied by differential seanning calorimetry. It is shown that in thermal denaturation process alcoholic leached soy protein concentrate(SPC) had more solid conformation and less rupture of conformaional linkage than aqueous acidic leached SPC. Water was of promotion to the thermal denaturation. With the increase of moisture content,the denaturation teniperatures of alcoholic leachecl SPC decrase steadily.Texturization of the protein was achieved by modifing the PH value of extrusion feed . which resulted in the increase of enthalpy related to thermal denaturaion. Physical and rheological properties of extrudates were finally improved effectivly.
Keywords:Extrusion  Protein denaturation  Differential seanning calorimetry  
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