Optimisation of bovine β-lactoglobulin hydrolysis using cardosins from dried flowers of Cynara cardunculus. (30th May 2021)

• Record Type: Journal Article
• Authors: Estévez, Natalia; Fuciños, Pablo; Fuciños, Clara; Rúa, María Luisa
• Is Part Of: Food chemistry. Volume 345(2021)
• Publication Date: 2021-05-30
• Subjects: Whey protein -- Purification -- Rate of hydrolysis -- Enzyme -- ACE-inhibitory activity -- Antioxidant activity; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.128741
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Cardosins A and B were purified from dried flowers of Cynara cardunculus. Bovine whey protein was hydrolysed with purified cardosins at different E/S ratios. High hydrolysis rates of β-Lg and α-La were achieved with cardosins at 1/150 U/mg. Biological activities of the hydrolysates were preliminarily studied. Abstract: Bovine whey protein was hydrolysed using cardosins A and B purified from dried flowers of Cynara cardunculus by combining diafiltration, anion-exchange chromatography and ultrafiltration. The proteolysis experiments were performed using different whey protein concentrations and enzyme/substrate (E/S) ratios. Complete hydrolysis of the main whey proteins, β-Lactoglobulin (β-Lg) and α-lactalbumin (α-La), was achieved after 4 h, at E/S ratios of 1/150 U/mg, regardless the initial protein concentration. In previous reports, the authors suggested that cardosins could not hydrolyse β-lactoblogulin. However, our promising results open up new possibilities to further explore the action of cardosins on whey proteins for the production of bioactive peptides.