![]() The native and heated WPC were incubated for 120 min with each level of pepsin and then used for tryptic hydrolysis. After peptic hydrolysis, the pepsin was inactivated by heating (at 90☌ for 10 min) in a water bath. The native and heated WPC solutions were incubated at 50☌ for 30, 60, 90, or 120 min with 0.1, 0.5, or 1% pepsin on a protein-equivalent basis. Native and heated WPC solutions were adjusted to pH 2 by addition of 0.5 N HCl for peptic hydrolysis. Further research is warranted to identify the low molecular weight small peptides in the WPC hydrolysates produced by pepsin and trypsin, which may enhance the use of whey. These results suggested that incubation of heated WPC with 1% pepsin and then with 1% trypsin was the most effective for producing low-antigenic hydrolysates by WPC hydrolysis and obtaining low molecular weight small peptides. The lowest antigenicity was observed when heated WPC was incubated with 1% pepsin and then with 1% trypsin. A low antigenic response was observed in heated WPC compared with native WPC. Antigenicity in heated and native WPC was reduced with an increasing level of enzymes. Antigenicity reversibly mimicked the hydrolysis of WPC and the removal of β-lactoglobulin from hydrolysates. The β-lactoglobulin in heated WPC was partially hydrolyzed by the 0.1 and 0.5% pepsin and trypsin treatments and was completely degraded by the 1% pepsin and trypsin treatment. ![]() The β-lactoglobulin in native WPC was not affected by the pepsin and trypsin treatments. Incubation of native WPC with 1% pepsin and then with 1% trypsin for 30 min completely removed the BSA and α-lactalbumin. The α-lactalbumin in native WPC was slightly degraded when incubated with 0.1% pepsin and then with 0.1% trypsin however, it was almost completely hydrolyzed within 60 min of incubation with 0.5% pepsin and then with 0.5% trypsin. High molecular weight bands, such as BSA, were completely eliminated from sodium dodecyl sulfate-PAGE of both native and heated WPC hydrolysates produced with pepsin for the 30-min incubation. The highest hydrolysis (25.23%) was observed in heated WPC incubated with 1% pepsin and then with 1% trypsin for 120 min. Hydrolysis of WPC was increased with an increasing level of enzymes and higher incubation times. A greater degree of hydrolysis was achieved and greater nonprotein nitrogen concentrations were obtained in heated WPC than in native WPC at all incubation times. ![]() Native and heated (10 min at 100☌) WPC (2% protein solution) were incubated at 50☌ for 30, 60, 90, and 120 min with 0.1, 0.5, and 1% pepsin and then with 0.1, 0.5, and 1% trypsin on a protein-equivalent basis. This study examined the effects of enzymes on the production and antigenicity of native and heated whey protein concentrate (WPC) hydrolysates. ![]()
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