Savinase, the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties

J Agric Food Chem. 2014 May 7;62(18):4166-74. doi: 10.1021/jf500849u. Epub 2014 Apr 28.

Abstract

The aim of this study was to produce multifunctional hydrolysates from lentil protein concentrates. Four different proteases (Alcalase, Savinase, Protamex, and Corolase 7089) and different hydrolysis times were evaluated for their degree and pattern of proteolysis and their angiotensin I-converting enzyme (ACE) inhibitory and antioxidant activities. Alcalase and Savinase showed the highest proteolytic effectiveness (P ≤ 0.05), which resulted in higher yield of peptides. The hydrolysate produced by Savinase after 2 h of hydrolysis (S2) displayed the highest ACE-inhibitory (IC50 = 0.18 mg/mL) and antioxidant activity (1.22 μmol of Trolox equiv/mg of protein). Subsequent reverse-phase HPLC-tandem mass spectrometric analysis of 3 kDa permeates of S2 showed 32 peptides, mainly derived from convicilin, vicilin, and legumin containing bioactive amino acid sequences, which makes them potential contributors to ACE-inhibitory and antioxidant activities detected. The ACE-inhibitory and antioxidant activities of S2 were significantly improved after in vitro gastrointestinal digestion (P ≤ 0.05). Multifunctional hydrolysates could encourage value-added utilization of lentil proteins for the formulation of functional foods and nutraceuticals.

Keywords: ACE-inhibitory peptides; alkaline proteases; antioxidant peptides; lentil protein hydrolysates.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrolysis
  • Lens Plant / chemistry*
  • Peptide Hydrolases / chemistry*
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Plant Proteins / chemistry*
  • Seeds / chemistry
  • Tandem Mass Spectrometry

Substances

  • Peptides
  • Plant Proteins
  • Peptide Hydrolases