Physical, chemical and biochemical properties of casein hydrolyzed by three proteases: Partial characterizations

•Sodium caseinate was hydrolyzed by three enzymes with different durations.•Solubility was greatly improved, becoming pH-independent after 24-h hydrolysis.•Emulsifying properties were generally enhanced after hydrolysis.•Antioxidant activities were dramatically elevated, except metal ion chelating a...

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Bibliographic Details
Published in:Food chemistry 2014-07, Vol.155, p.146-154
Main Authors: Luo, Yangchao, Pan, Kang, Zhong, Qixin
Format: Article
Language:English
Subjects:
ACE-inhibitory activity
Angiotensin-Converting Enzyme Inhibitors - chemistry
Antioxidant activity
Biological and medical sciences
Caseins - chemistry
Chelating Agents - chemistry
Emulsifying property
Food toxicology
Hydrolysates
Hydrolysis
Medical sciences
Pancreatin - chemistry
Papain - chemistry
Proteases
Protein Hydrolysates - chemistry
Sodium caseinate
Toxicology
Trypsin - chemistry
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Summary:•Sodium caseinate was hydrolyzed by three enzymes with different durations.•Solubility was greatly improved, becoming pH-independent after 24-h hydrolysis.•Emulsifying properties were generally enhanced after hydrolysis.•Antioxidant activities were dramatically elevated, except metal ion chelating activity.•ACE-inhibitory activity was improved up to 9times of sodium caseinate. Sodium caseinate (NaCas) was hydrolyzed by papain, pancreatin and trypsin from 10min to 24h, and the hydrolysates were partially characterized for several important properties. At the studied conditions, papain and trypsin were more effective in hydrolyzing NaCas than pancreatin. Pancreatin treatments showed an initial increase in surface hydrophobicity, contrasting with the consistent decrease for the other two treatments. The solubility of NaCas at acidic pH was improved, becoming pH-independent after 24h hydrolysis. The emulsifying properties generally showed improvements after hydrolysis. The DPPH free radical scavenging activity, reducing power, and inhibition of linoleic acid autoxidation were significantly enhanced after appropriate hydrolysis, while metal ion chelating effects were slightly attenuated. The angiotensin converting enzyme-inhibitory activity was significantly improved by up to 9times than that of NaCas. These findings indicate that physical, chemical and biochemical properties of casein hydrolysates can be improved by selecting proteolytic conditions to produce functional ingredients.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2014.01.048