Angiotensin-I converting enzyme inhibitory and antioxidant activities of protein hydrolysates from Phaseolus lunatus and Phaseolus vulgaris seeds

• Published in: Food science & technology 2009-12, Vol.42 (10), p.1597-1604
• Main Authors: Torruco-Uco, Juan, Chel-Guerrero, Luis, Martínez-Ayala, Alma, Dávila-Ortíz, Gloria, Betancur-Ancona, David
• Format: Article
• Language: English
• Subjects: ACE-I inhibitors; angiotensin I; antihypertensive effect; Antioxidant activity; enzyme inhibitors; free radical scavengers; health promotion; legume protein; molecular weight; P. lunatus; P. vulgaris; Phaseolus lunatus var. lunatus; Phaseolus vulgaris; Protein hydrolysates
• ISSN: 0023-6438; 1096-1127
• DOI: 10.1016/j.lwt.2009.06.006

Phaseolus lunatus and Phaseolus vulgaris protein concentrates were hydrolyzed with the enzymes Alcalase ® and Flavourzyme ® at different reaction times, and the angiotensin-I converting enzyme (ACE-I) inhibitory activity, antioxidant properties and amino acid composition measured in the hydrolysates. With Alcalase ®, the highest degree of hydrolysis (DH) in P. lunatus was 37.94% at 45 min, and in P. vulgaris was 49.48% at 30 min. With Flavourzyme ®, the highest DH's were 22.03% and 26.05%, respectively, both at 90 min. ACE-I inhibitory activity in the Alcalase ® hydrolysates was IC 50 = 0.056 mg mL −1 for P. lunatus at 90 min, and IC 50 = 0.061 mg mL −1 for P. vulgaris at 60 min. In the Flavourzyme ® hydrolysates this activity was IC 50 = 0.0069 mg mL −1 for P. lunatus at 90 min and IC 50 = 0.127 mg mL −1 for P. vulgaris at 45 min. In SDS-PAGE, the hydrolysates exhibited low molecular weight bands. Antioxidant activity was 11.55 mmol L −1 TEAC mg −1 protein for P. lunatus with Flavourzyme ® at 90 min and 10.09 mmol L −1 TEAC mg −1 protein for P. vulgaris with Alcalase ® at 60 min. Amino acid composition exhibited high amino acid hydrophobic residues content.