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Reaction Kinetics of Gliadin Glutenin Cross-Linking in Model Systems and in Bread Making

机译:麦醇溶蛋白谷蛋白交联在模型系统和面包制备中的反应动力学

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摘要

The gluten proteins gliadin and glutenin are important for wheat flour functionality in bread making, where, during baking, they polymerize through a heat-induced sulfhydryl—disulfide exchange mechanism. A model system was used to study the kinetics of this reaction. Thus, gluten was subjected to hydrothermal treatment with the rapid visco analyzer (RVA) with holding temperatures of 80, 90, and 95 °C. At these temperatures, ω-gliadin solubility did not change, but the solubilities of α- and γ-gliadin in 60% ethanol decreased according to first-order reaction kinetics. All reaction rate constants increased with temperature. The activation energies for the heat-induced exchange reaction were 110 and 147 kJ/mol for α- and γ-gliadin, respectively. Starch did not influence the reaction rates of the association of α- and γ-gliadin with glutenin. During gluten-starch model bread baking, glutenin oxidized first, and when the internal crumb temperature reached 100 °C, α- and γ-gliadin cross-linked to glutenin, again following first-order reaction kinetics. The experimental findings and similarities in temperature conditions and reaction kinetics suggest that the RVA system can be instrumental in understanding gluten behavior in concentrated food systems, such as bread making.
机译:面筋蛋白麦醇溶蛋白和谷蛋白在面包制造中对于小麦面粉功能至关重要,在烘烤过程中,它们通过热诱导的巯基-二硫化物交换机制聚合。使用模型系统研究该反应的动力学。因此,使用快速粘度分析仪(RVA)对面筋进行水热处理,保持温度为80、90和95°C。在这些温度下,ω-麦醇溶蛋白的溶解度没有变化,但是α-和γ-麦醇溶蛋白在60%乙醇中的溶解度根据一级反应动力学而降低。所有反应速率常数均随温度增加。对于α-和γ-麦醇溶蛋白,热诱导交换反应的活化能分别为110和147 kJ / mol。淀粉不影响α-和γ-麦醇溶蛋白与谷蛋白的缔合反应速率。在面筋-淀粉模型面包烘烤过程中,面筋首先被氧化,当内部面包屑温度达到100°C时,α-和γ-麦醇溶蛋白交联到面筋上,再次遵循一级反应动力学。实验结果以及温度条件和反应动力学的相似性表明,RVA系统有助于理解浓缩食品系统(例如面包制作)中的面筋行为。

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