期刊
FOOD CHEMISTRY
卷 171, 期 -, 页码 224-232出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.08.116
关键词
Lentil peptides; High-hydrostatic pressure; Angiotensin I converting enzyme; Antioxidant activity; Proteolysis
资金
- Spanish Ministry of Economy and Competitiveness (MINECO - Spain) [AGL2010-16310]
Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention due to their beneficial effects in the prevention/treatment of hypertension. The objective was to explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the release of bioactive peptides from lentil proteins. Pressurisation (100-300 MPa) enhanced the hydrolytic efficiency of Protamex, Savinase and Corolase 7089 compared to Alcalase. Proteolysis at 300 MPa led to a complete degradation of lentil proteins and increased peptide (<3 kDa) concentration by all enzymes. Proteolysis at 300 MPa by Savinase gave rise to lentil hydrolysates (S300) with the highest ACE-inhibitory and antioxidant activities that were retained upon in vitro gastrointestinal digestion. The peptides responsible for the multifunctional properties of S300 hydrolysate were identified as different fragments from storage proteins and the allergen Len c 1. These results support the potential of HP as a technology for the cost-effective production of bioactive peptides from lentil proteins during enzymatic proteolysis. (C) 2014 Elsevier Ltd. All rights reserved.
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