Commercial isolated yellow field pea protein isolate (IPP) was subjected to 200, 400 and 600 MPa high hydrostatic pressure (HHP) treatments followed by determination of some physicochemical and functional properties. Native polyacrylamide gel electrophoresis confirmed HHP-induced formation of high molecular weight protein aggregates. Intrinsic fluorescence showed most intense at 600 MPa where fluorescence intensity was less than half of the control IPP. The 600 MPa-treated IPP also showed more unfolded structure with an extensive red shift (384 nm) in wavelength of maximum tryptophan fluorescence. However, solubility profile was very similar and was not significantly (p > 0.05) affected by HHP treatment. At pH 3.0, HHP-treated IPP formed significantly (p < 0.05) higher quality emulsions with oil droplet sizes (d_4,3) of 26–68 μm when compared to 52–92 μm for the control IPP. Foaming capacity was also higher at pH 3.0 with a maximum value of 81% when compared to maximum values of 38% and 62% obtained, respectively at pH 5.0 and 7.0.

对商业分离的黄豌豆蛋白质分离物（IPP）进行200、400和600 MPa的高静水压（HHP）处理，然后确定一些理化和功能特性。天然聚丙烯酰胺凝胶电泳证实了HHP诱导的高分子量蛋白质聚集体的形成。本征荧光在600 MPa时表现出最强的强度，其中荧光强度小于对照IPP的一半。经600 MPa处理的IPP还显示出更多的未折叠结构，最大色氨酸荧光的波长发生了广泛的红移（384 nm）。但是，溶解度曲线非常相似，并且 不受HHP处理的影响（p > 0.05）。在pH 3.0时，经过HHP处理的IPP明显形成（p <0.05）更高质量的乳剂，油滴尺寸（d _4,3）为26–68μm，而对照IPP为52–92μm。与在pH 5.0和7.0分别获得38％和62％的最大值相比，在pH 3.0处的发泡能力也更高，最大值为81％。