Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate
Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate
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DOI：
10.1111/j.1365-2621.1996.tb14174.x
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发表时间：
1996-03-01
影响因子：
3.9
通讯作者：
Kilara, A
中科院分区：
文献类型：
--
作者：
Mutilangi, WAM;Panyam, D;Kilara, A
用胰蛋白酶、α-胰凝乳蛋白酶、Alcalase或Neutrase将热变性乳清蛋白分离物水解至2.8、4.3、6.0或8.0%的水解度。水解产物通过超滤分级并冷冻干燥。截留物的蛋白质含量变化不大，但渗透物与酶不同。表面疏水性增加，水解，但不是线性的，除了铬-糜蛋白酶。超滤增加了溶解度，渗透物和截留物比水解物具有更好的溶解度。截留物的乳化活性指数高于水解物，而渗透物不能形成稳定的乳状液。渗透物形成稳定的泡沫，但水解产物和渗余物显示出差的发泡特性。酶的特异性和水解度影响肽的功能性质。在所有水解水平下，胰蛋白酶产生的级分通常具有较高的溶解度、乳化性和发泡性。Alcalase水解的渗透液具有最好的泡沫容量，但泡沫稳定性较低。
Heat-denatured whey protein isolate was hydrolyzed with trypsin, alpha-chymotrypsin, Alcalase or Neutrase to 2.8, 4.3, 6.0 or 8.0% degree of hydrolysis. Hydrolysates were fractionated by ultrafiltration and freeze-dried. Protein content of retentates showed little variation but permeates differed with enzyme. Surface hydrophobicity increased with hydrolysis but was not linear except for cr-chymotrypsin. Ultrafiltration increased solubility and the permeates and retentates had better solubility than hydrolysates. Retentates had higher emulsifying activity index than hydrolysates while permeates did not form stable emulsions. permeates formed stable foams but hydrolysates and retentates showed poor foaming characteristics. Specificity of the enzyme, and degree of hydrolysis influenced the functional properties of the peptides. Fractions generated by trypsin, at all levels of hydrolysis generally had higher solubility, emulsifying properties and foaming properties. Permeates from Alcalase hydrolysis had the best foam capacity but low foam stability.