Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, PR China.
Food Funct. 2019 Mar 20;10(3):1653-1660. doi: 10.1039/c8fo01880d.
Whey protein isolate (WPI) was hydrolyzed by alcalase and trypsin for three hydrolysis degrees (DHs), followed by transglutaminase (TGase) induced cross-linking. The prepared products were measured for surface hydrophobicity and emulsifying and foaming properties, as well as in vitro antigenicity for α-lactalbumin and β-lactoglobulin. The results indicated that enzymatic hydrolysis of WPI mostly resulted in WPI hydrolysates with significantly decreased antigenicity of α-lactalbumin and β-lactoglobulin, especially in the case of a higher DH value. Moreover, the TGase-induced cross-linking led to a further antigenicity decrease for these prepared products. Alcalase was always more potent than trypsin to decrease antigenicity. In comparison with WPI, the conducted enzymatic hydrolysis also brought losses to surface hydrophobicity and emulsifying and foaming properties. On the other hand, the conducted cross-linking could partially rescue these properties. It is thus concluded that the assessed enzymatic hydrolysis coupled with TGase-induced cross-linking might be an applicable process for WPI to decrease its potential antigenicity but reserve partial interfacial properties.
乳清蛋白分离物（WPI）分别用碱性蛋白酶和胰蛋白酶进行水解，达到三个水解度（DH），然后用转谷氨酰胺酶（TGase）诱导交联。测定了所得产物的表面疏水性、乳化和泡沫性能以及α-乳白蛋白和β-乳球蛋白的体外抗原性。结果表明，WPI 的酶解主要导致 WPI 水解产物的α-乳白蛋白和β-乳球蛋白的抗原性显著降低，特别是在更高的 DH 值的情况下。此外，TGase 诱导的交联导致这些制备产物的抗原性进一步降低。碱性蛋白酶比胰蛋白酶更能有效降低抗原性。与 WPI 相比，酶解也导致表面疏水性和乳化及泡沫性能损失。另一方面，进行交联可以部分恢复这些性能。因此，可以得出结论，评估的酶解结合 TGase 诱导的交联可能是 WPI 降低其潜在抗原性但保留部分界面性能的一种可行工艺。
