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作 者:杨玉玲[1] 董秋颖[1] 王素雅[1] 董哲[1] 马云[1] 朱冰[1]
机构地区:[1]南京财经大学食品科学与工程学院,江苏南京210003
出 处:《食品科学》2011年第1期1-4,共4页Food Science
基 金:国家自然科学基金项目(31071570);江苏省自然科学基金项目(KB2006175)
摘 要:以凝胶硬度和贮能模量G'为指标,通过添加不同试剂,研究明胶-肌原纤维蛋白混合凝胶形成的作用力。添加尿素能显著降低混合凝胶的硬度,说明在低温下,氢键是凝胶形成和维持的最重要作用力。改变pH值、添加DTT和溴酸钾、添加SDS均导致凝胶硬度发生变化,说明静电相互作用、二硫键和疏水相互作用对凝胶的形成和维持都起到了一定作用。在加热过程中,混合样品的G'随pH值增加而降低;添加DTT、SDS和尿素均导致混合样品的G'下降;由于添加SDS导致G'下降最为显著,因此,疏水相互作用在混合样品形成热诱导凝胶中起到最重要的作用。The values of gel hardness and storage modulus G' of compound gelatin-myofibrillar protein gels formed in the attendance of different reagents were measured in order to understand the forces involved in the gel formation.It was found that adding urea distinctly decreased gel hardness.This suggests that hydrogen bond is the most important force responsible for gel formation and maintenance at low temperatures.Gel hardness could be changed by adjusting pH or by separately adding DTT,potassium bromate or SDS,indicating all electrostatic force,disulfide bond and hydrophobic interaction make a contribution to gel formation and maintenance.Increasing pH during heating treatment resulted in a lower G' value.Additions of DTT,SDS and urea were all able to decrease G'value,and the most obvious decrease was observed when SDS was added.Therefore,it can be concluded that hydrophobic interaction plays the most vital role in the heat-induced gel formation between gelatin and myofibrillar.
分 类 号:TS201.7[轻工技术与工程—食品科学]
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