A soy protein isolate was hydrolyzed with Alcalase®, Flavourzyme® and their combination, and the resulting hydrolysates (A, F and A + F) were ultrafiltered and analyzed through SDS-PAGE. Fractions with MW < 1 kDa were investigated for their ACE-inhibitory activity, and the most active one (A < 1 kDa) was purified by semi-preparative RP-HPLC, affording three further subfractions. NMR analysis and Edman degradation of the most active subfraction (A1) enabled the identification of four putative sequences (ALKPDNR, VVPD, NDRP and NDTP), which were prepared by solid-phase synthesis. The comparison of their ACE-inhibitory activities suggested that the novel peptide NDRP might be the main agent responsible for A1 fraction ACE inhibition (ACE inhibition = 87.75 ± 0.61%; IC50 = 148.28 ± 9.83 μg mL-1). NDRP acts as a non-competitive inhibitor and is stable towards gastrointestinal simulated digestion. The Multiple Reaction Monitoring (MRM) analysis confirmed the presence of NDRP in A < 1 kDa.

Preparation, Characterization and In Vitro Stability of a Novel ACE-Inhibitory Peptide from Soybean Protein / S. Sangiorgio, N. Vidović, G. Boschin, G. Aiello, P. Arcidiaco, A. Arnoldi, C.F. Morelli, M. Rabuffetti, T. Recca, L. Scarabattoli, D. Ubiali, G. Speranza. - In: FOODS. - ISSN 2304-8158. - 11:17(2022 Sep 01), pp. 2667.1-2667.14. [10.3390/foods11172667]

Preparation, Characterization and In Vitro Stability of a Novel ACE-Inhibitory Peptide from Soybean Protein

S. Sangiorgio
Primo
;
G. Boschin;C.F. Morelli;M. Rabuffetti;T. Recca;L. Scarabattoli;G. Speranza
Ultimo
2022

Abstract

A soy protein isolate was hydrolyzed with Alcalase®, Flavourzyme® and their combination, and the resulting hydrolysates (A, F and A + F) were ultrafiltered and analyzed through SDS-PAGE. Fractions with MW < 1 kDa were investigated for their ACE-inhibitory activity, and the most active one (A < 1 kDa) was purified by semi-preparative RP-HPLC, affording three further subfractions. NMR analysis and Edman degradation of the most active subfraction (A1) enabled the identification of four putative sequences (ALKPDNR, VVPD, NDRP and NDTP), which were prepared by solid-phase synthesis. The comparison of their ACE-inhibitory activities suggested that the novel peptide NDRP might be the main agent responsible for A1 fraction ACE inhibition (ACE inhibition = 87.75 ± 0.61%; IC50 = 148.28 ± 9.83 μg mL-1). NDRP acts as a non-competitive inhibitor and is stable towards gastrointestinal simulated digestion. The Multiple Reaction Monitoring (MRM) analysis confirmed the presence of NDRP in A < 1 kDa.
ACE inhibitor; Lineweaver–Burk plot; functional food; peptide synthesis; simulated gastrointestinal digestion; soybean protein hydrolysate;
Settore CHIM/06 - Chimica Organica
Settore CHIM/10 - Chimica degli Alimenti
CAR_RIC18GSPER_01 - Biocatalysis for oils and fats in cosmetics (BioCosm) - SPERANZA, GIOVANNA - CAR_RIC - Bandi Fondazione Cariplo - 2018
https://www.mdpi.com/2304-8158/11/17/2667
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/938466
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