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首页> 外文期刊>Journal of Food Science and Technology >Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde.
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Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde.

机译:丙二醛氧化修饰对大豆蛋白热聚集和凝胶特性的影响。

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摘要

Malondialdehyde (MDA) was selected as a representative of lipid peroxidation products to investigate the effects of oxidative modification on thermal aggregation and gel properties of soy protein by lipid peroxidation products. Incubation of soy protein with increasing concentration of MDA resulted in gradual decrease of particle size and content of thermal aggregates during heat denaturation. Oxidative modification by MDA resulted in a decrease in water holding capacity, gel hardness, and gel strength of soy protein gel. An increase in coarseness and interstice of MDA modified protein gel network was accompanied by uneven distribution of interstice as MDA concentration increased. The results showed that degree of thermal aggregation of MDA-modified soy protein gradually decreased as MDA concentration increased, which contributed to a decrease in water holding capacity, gel hardness, and gel strength of MDA-modified soy protein gel
机译:选择丙二醛(MDA)作为脂质过氧化产物的代表,以研究氧化修饰对脂质过氧化产物对大豆蛋白的热聚集和凝胶性质的影响。随着MDA浓度的增加,大豆蛋白的孵育会导致热变性过程中粒度和热聚集物含量逐渐降低。 MDA的氧化修饰导致大豆蛋白凝胶的持水量,凝胶硬度和凝胶强度降低。随着MDA浓度的增加,MDA修饰的蛋白质凝胶网络的粗糙度和空隙增加,同时空隙分布不均匀。结果表明,MDA改性大豆蛋白凝胶的热聚集程度随着MDA浓度的增加而逐渐降低,这导致MDA改性大豆蛋白凝胶的持水量,凝胶硬度和凝胶强度降低。

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