Production of whey protein hydrolysates with angiotensin-converting enzyme-inhibitory activity using three new sources of plant proteases

Abstract

Abstract Production of functional/bioactive components by whey protein hydrolysis using new plant proteases represents an innovative area in food processing and functional foods. The present study evaluated the potential use of plant crude extracts from Citrus aurantium flowers, trompillo (Solanum elaeagnifolium) berries (TE) and melon (Cucumis melo) fruit (ME) for production of whey protein hydrolysates. The hydrolytic patterns of whey proteins (i.e., β-lactoglobulin, α-lactalbumin, serum albumin, and immunoglobulins) at pH 3.5 and 6.5, at 0, 3, 6, 9, and 24 h, were monitored by HPLC and SDS-PAGE analysis. Maximum proteolytic action on the major whey proteins (i.e., β-lactoglobulin and α-lactalbumin) was obtained using ME and TE at pH 6.5. Whey hydrolysates that presented more hydrolysis of β-lactoglobulin showed the highest angiotensin-converting enzyme inhibitory activities (75–90% inhibition). The use of these new plant proteases offers potential in the production of hydrolysates with bioactive properties for the development of functional foods.