Color and structural modifications of alkaline extracted sunflower protein concentrates and isolates using L-cysteine and glutathione

Abstract

Alkaline sunflower protein extraction can be performed along with de-phenolization of sunflower seed proteins if greening is unwanted. This greening is promoted at alkaline pH when chlorogenic acid (CGA) oxidizes and reacts with amino acids such as lysine. Thiol-containing dough conditioners: L-cysteine hydrochloride and glutathione (GSH) were investigated as an alternative de-greening strategy to acidification and de-phenolization. Greening and browning inhibition of thiols (GSH and Cysteine) were modeled by a combination of additive and interaction effects of extraction pH (7.0 to 11.0) and thiol concentration (0.00 to 5.60 mM) randomly assigned by Response Surface Methodology (RSM). The powders with the highest greening were the controls (pH 8.9-9.3 and no added thiols) and powders at pH 10.41 with 0.82 mM thiols. From RSM, the maximum greening inhibition was achieved at pH 8.71 and 4.23 mM cysteine, and pH 8.51 and 3.78 mM GSH. However, cysteine caused more browning at alkaline pH than GSH. Furthermore, fluorescence spectroscopy showed that cysteine had a protective effect against alkaline unfolding, whereas GSH quenched fluorescence in a concentration-dependent manner. Overall, de-greening of alkaline extracted sunflower protein was achieved by adding cysteine or glutathione, but the thiols differed in their contribution to the browning and unfolding effect.

Keywords: Cysteine; Fluorescence quenching; Glutathione; Greening; Sunflower-protein.