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作 者:李杨[1] 李秋慧[1] 王海晴[1] 王中江[1] 冯志权 江连洲[1]
出 处:《中国食品学报》2015年第11期41-47,共7页Journal of Chinese Institute Of Food Science and Technology
基 金:黑龙江省教育厅科学技术研究项目(12531049)
摘 要:通过对大豆分离蛋白-磷脂酶解产物乳状体系的共建,探究不同磷脂酶A1,A2,C,D酶解磷脂对乳化体系乳化性质的影响,测定添加不同磷脂酶解产物后蛋白乳化体系的可溶性蛋白含量、乳化活性、乳化稳定性、乳层析指数、Zeta电位、粒径分布、光学显微镜的变化。结果表明,磷脂酶解产物与大豆分离蛋白有明显的交互作用,其中磷脂经磷脂酶A2酶解后的产物与大豆分离蛋白共建的乳化体系,在乳化活性、稳定性、粒径分布、Zeta电位、显微结构方面均好于其它复合体系。其乳化活性提高10.17 m2/g,稳定性提高25.2%,负Zeta电位绝对值增加5.09 m V,乳状液平均粒径明显变小,显微结构乳滴分布均匀。这表明经磷脂酶A2酶解后的磷脂非极性基团减少,亲水性增强,与蛋白交互作用增强,使蛋白更好的结合到磷脂的片层结构中,改变复合物结构,促进乳化体系稳定。In order to determine the effects of phospholipase A1, A2, C, D hydrolysates on the emulsification system properties and the corresponding mechanism, the title built the soybean isolate protein-phospholipase hydrolysis production emulsion system and each emulsion system emulsified activity, emulsion stability, creaming index, soluble protein content, particle size distribution, Zeta potential, optical microscope were investigated. The results showed that the Phospholipase hydrolysis production occured more obvious interaction with soybean protein isolate, especially phospholipids by phospholipase A2, which enhanced much better in emulsifying activity, stability, particle size distribution, Zeta potential,microscopic structure than the other products of enzymatic hydrolysis. The negative Zeta potential of emulsion system increased in absolute value, the emulsion particle size smaller, emulsifying activity and stability are improved obviously.This change explained the phospholipid enzymed by phospholipase A2 caused the phospholipid non-polar groups decreased, and the enhancement of hydrophilicities, changed protein and phospholipid structure so that the interaction between protein and phospholipid became stronger.
分 类 号:TS201.2[轻工技术与工程—食品科学]
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