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Black bean (Phaseolus vulgaris L.) protein hydrolysates: Physicochemical and functional properties
•Pepsin-treated protein had higher hydrolysis degree than the alcalase-treated protein.•Alcalase-treated hydrolysates showed higher purity and hydrophobicity.•Alcalase-treated hydrolysates presented higher emulsion stability than pepsin digestion.•Protein concentrate and hydrolysates had antioxidant...
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Published in: | Food chemistry 2017-01, Vol.214, p.460-467 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Pepsin-treated protein had higher hydrolysis degree than the alcalase-treated protein.•Alcalase-treated hydrolysates showed higher purity and hydrophobicity.•Alcalase-treated hydrolysates presented higher emulsion stability than pepsin digestion.•Protein concentrate and hydrolysates had antioxidant activity.
Black bean protein hydrolysates obtained from pepsin and alcalase digestions until 120min of hydrolysis were evaluated by gel electrophoresis, relative fluorescence intensity, emulsifying properties, light micrograph of emulsions and in vitro antioxidant activity. The emulsion stability of the bean protein hydrolysates were evaluated during 30days of storage. The pepsin-treated bean protein hydrolysates presented higher degree of hydrolysis than the alcalase-treated protein hydrolysates. The alcalase-treated bean protein hydrolysates showed higher surface hydrophobicity. Moreover, the protein hydrolysates obtained with alcalase digestion presented higher emulsion stability during 30-days than those obtained from pepsin digestion. The protein concentrate and especially the hydrolysates obtained from alcalase digestion had good emulsion stability and antioxidant activity. Thus, they could be exploited as protein supplements in the diet as nutritional and bioactive foods. |
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ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2016.07.046 |