Effects of succinylation and deamidation on functional properties of oat protein isolate

Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

“…Similarly, the present evaluation also showed that GC-CN had better solubility than caseinate (Figure 2). Deamidation of glutamine and asparagine residues leads to increased protein solubility, due to an increase in net charges (Mirmoghtadaie, Kadivar, & Shahedi, 2009) and electrostatic repulsion (Claughton & Pearce, 1989). These results supported that GC-DCN1 and especially GC-DCN2 had better solubility than GC-CN (Figure 2), mainly due to the increased ionizable carboxylic groups in their molecules (Figure 3).…”

Application Potential of Food Protein Modification

“…Other effects observed upon charge modification of proteins are related to emulsification properties: methylation increased while succinylation decreased the emulsifying activity of rapeseed preparations (Dua et al, 1996). Other studies show an increased emulsifying activity and stability upon succinylation of soy protein (Franzen & Kinsella, 1976a), and oat protein isolate (Mirmoghatadaie et al, 2009). In terms of gelation, an increase in net charge lead to more transparent gels upon gelation of ovalbumin which is related to the morphology of the aggregated network making up the gel structure (Weijers et al, 2008).…”

“…Other functional properties are equally affected by succinylation. For example, protein solubility has been reported to increase upon succinylation as has been demonstrated for rapeseed preparations (Dua et al, 1996), flax protein isolate (Wanasundara & Shahidi, 1997), oat protein isolate (Mirmoghatadaie et al, 2009), and soy protein isolate (Franzen & Kinsella, 1976a). Improved solubility has been related to the ability of proteins to perform more efficiently as stabilizers in emulsions and foams (Nakai & Li-Chan, 1988;Waniska & Kinsella, 1979), which, in turn, is greatly affected by their ability to absorb at the air-water interface (Wierenga et al, 2005).…”

“…Improved solubility has been related to the ability of proteins to perform more efficiently as stabilizers in emulsions and foams (Nakai & Li-Chan, 1988;Waniska & Kinsella, 1979), which, in turn, is greatly affected by their ability to absorb at the air-water interface (Wierenga et al, 2005). It has indeed been shown that treatment of a variety of proteins with succinic anhydride leads to increased foam capacity (Dua et al, 1996;Franzen & Kinsella, 1976a;Mirmoghatadaie et al, 2009), although others suggest that succinylation leads to decreased foam expansion capacity (Wanasundara & Shahidi, 1997). These seemingly contradictive findings may be explained by the demonstration by Wierenga and colleagues (2005) that the likelihood of a protein molecule to adsorb at an interface is the result of a balance between hydrophobic and steric effects: highly charged molecules may be adsorbing to the interface as a result of hydrophobic interaction, but the density at which protein molecules continue adsorbing to the interface is mainly determined by the repulsive nature of the charged proteins.…”

Preparation of microwave-phosphorylated soy protein isolates through a Box–Behnken model optimization

“…Adequate modification on SPI might improve its functional properties and applications in the food industry. Physical (Puppo, Chapleau, Speroni, de Lamballerie, An˜o´n, & Anton, 2004), chemical (Mirmoghtadaie, Kadivar, & Shahedi, 2009), and enzymatic modification (Suro´wka & _ Zmudzin´ski, 2004) had been used to improve emulsifying properties of SPI. Chemical modification including acylation, phosphorylation, glycosylation, deaminization, and covalent cross-linking were used mostly (Moure, Sineiro, & Domı´nguez, 2006).…”