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

作者：Torruco Uco Juan; Chel Guerrero Luis; Martinez Ayalac Alma; Davila Ortiz Gloria; Betancur Ancona David^*

来源：LWT-Food Science and Technology, 2009, 42(10): 1597-1604.

DOI：10.1016/j.lwt.2009.06.006

• P. lunatus
• P. vulgaris
• Protein hydrolysates
• ACE-I inhibitors
• Antioxidant activity

Phaseolus lunatus and Phaseolus vulgaris protein concentrates were hydrolyzed with the enzymes Alcalase (R) and Flavourzyme (R) 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 (R), the highest degree of hydrolysis (DH) in P. lunatus was 37.94% at 45 min, and in R vulgaris was 49.48% at 30 min. With Flavourzyme (R), the highest DH's were 22.03% and 26.05%, respectively, both at 90 min. ACE-I inhibitory activity in the Alcalase (R) hydrolysates was IC(50) = 0.056 mg mL(-1) for P. lunatus at 90 min, and IC(50) = 0.061 mg mL(-1) for R vulgaris at 60 min. In the Flavourzyme (R) 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 R vulgaris at 45 min. In SIDS-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 (R) at 90 min and 10.09 mmol L(-1) TEAC mg(-1) protein for P. vulgaris with Alcalase (R) at 60 min. Amino acid composition exhibited high amino acid hydrophobic residues content.

• 出版日期2009-12