Effect of cysteine on structural, rheological properties and solubility of wheat gluten by enzymatic hydrolysis

Abstract

The progressive enzymatic hydrolysis of wheat gluten was obtained with Fourier transform infrared spectroscopy structural and rheological understanding of the molecular interactions and structural transformations as affected by cysteine. Cysteine which cleaved disulphide (SS) bonds and inhibited wheat gluten polymer formation induced the disappearance of 1622 cm )1 band (extended structures) and significant increases in the amount of b-sheet in the amide I region and in hydration capacity. The alterations in structure had tremendous influence on the rheological properties of wheat gluten so that decreased the shear moduli (loss modulus and storage modulus) and viscosity. A typical viscoelastic behaviour (ranging from more solid-like to more fluid-like) affected by cysteine was manifested by wheat gluten dough. Consequently, the solubility of wheat gluten improved. Hence, structural, rheological changes and solubility gave rise to high enzymatic hydrolysis of wheat gluten.

Efeitos de enxofre e nitrogênio na qualidade industrial e no rendimento de grãos de trigo

“…reversal with no significant magnitude. The positive correlation between L, W, and GLC only observed in the presence of sulfur, it is in accordance with the claims that nutrient supplementation improves the technological quality of bread dough due to an increase in proteins that form gluten as well as the best configuration of those provided by inter and intra molecular bonds of sulfur amino acid cysteine residue (ZHANG et al 2010).…”

Heat‐Induced Gelation Mechanism of Blood Plasma Modulated by Cysteine

“…Protein aggregation in the presence of Cys could be related to interactions of the disulfide bonds present in the plasma proteins via ‒SH/SS interchange reactions, which can occur at room temperature, and cause protein dissociation and/or unfolding (Singh ). Consequently the compactness of protein structure can decrease, with not only hidden polar groups becoming exposed by enhancing water–protein bonding (Mejri and others ; Zhang and others ), but also hydrophobic groups, this way promoting unspecific protein interaction (Li‐Chan and Nakai ) and favoring the hydrogen‐bond formation contributing to protein aggregation. The low intensity of the band aggregation can be due to the pH conditions used in this study, under which the disulphide bond cleavage should not be particularly enhanced.…”

“…Reducing agents with the ability to interact with disulfide bonds and/or free SH groups can sharply alter the heat‐induced gel properties of globular proteins by modifying the mechanisms governing the gelation process (Matsudomi and others ; Legowo and others ; Hoffman and van Mill ; Zhang and others ). Free‐thiol compounds like dithiothreitol (DTT), β‐mercaptoethanol, glutathione, and cysteine (Cys) are commonly used with such purpose.…”

The effect of redox agents on conformation and structure characterization of gluten protein: An extensive review

“…This induced an increase in gluten protein solubility at isoelectric point and other pH values (Zhang et al, 2010). Based on the FTIR data attained by Mejri et al (2005), β-turn and β-sheet increased,…”

“…Surface hydrophobicity decreased owing to the exposure of polar groups in polypeptide chains to the surface of gluten network and the breaking of intra-and interchain disulfide bonds in wheat gluten, hence the greater hydration capacity. Cysteine addition ameliorated extensibility, machinability, and adhesiveness and reduced the elastic (G′) and viscous (G″) characteristics, tolerance to mixing, and mixing time (Angioloni & Dalla Rosa, 2007;Indrani & Venkateswara Rao, 2006;Koh et al, 2005;Kumar et al, 2014;Lambert & Kokini, 2001;Manohar & Rao, 1997;Miller & Hoseney, 2008;Stoica et al, 2010;Yuno-Ohta et al, 2009;Zhang et al, 2010) Holler & Hopkins, 1989;Joye et al, 2009b;Koh et al, 1996Koh et al, , 2005Kumar et al, 2014;Lagrain et al, 2006Lagrain et al, , 2007Reinbold et al, 2008;Tilley et al, 2001;Zhang et al, 2010).…”