Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 64, Issue 8, Pages 1730-1740Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.5b06080
Keywords
pinto bean; high-pressure-assisted proteolysis; bioactive peptides; phenolic compounds; biological activity; reducing power; antioxidant activity
Funding
- Ministry of Economy and Competitiveness (MINECO, Spain) [AGL2010-16310, AGL2013-43247-R]
- FEDER program from the European Commission
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Pinto bean protein concentrate was hydrolyzed by subtilisins at 0.1, 100, and 200 MPa and 50 degrees C for 15 min. Alcalase hydrolysis at 100 MPa led to higher ACE inhibition, reducing power, and free radical scavenging activity of hydrolysates. However, hydrolysate obtained by Savinase at 200 MPa showed the best ACE-inhibitory and radical scavenging activities. Proteolysis by Savinase at 200 MPa was considered the most effective treatment to increase small peptides (<3 kDa), flavonoids, total phenolic compounds, and oxygen radical absorbance capacity in hydrolysates. In this hydrolysate, small phaseolin fragments with reported ACE-inhibitory and antioxidant sequences were identified. Catechin, pelargonidin 3-glucoside, and ferulic acid were the main phenolic compounds. Hihg-pressure-assisted hydrolysis of common bean protein concentrates would provide benefits in the production of functional hydrolysates providing higher functionality and added value to the resulting hydrolysate due to synergistic effects of bioactive peptides and soluble phenolics.
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