Combined treatment of porcine plasma with microbial transglutaminase and cysteine: Effects on the heat-induced gel properties

The effect of transglutaminase-induced polymerization in the presence of cysteine on β-lactoglobulin antigenicity

“…b-Lg and a-La are poor substrates for TG, although the reaction is facilitated after denaturation by heat treatment (>70 C) or by the addition of reducing agents such as dithiothreithol (DTT) or b-mercaptoethanol, which cleave disulfide bonds (Eissa, Puhl, Kadla, & Khan, 2006;Faergemand, Otte, & Qvist, 1997;Fort, Carretero, Paré s, & Toldra, 2007;Mahmoud & Savello, 1992). However, structural modification was only observed when the reaction occurred in the presence of DTT (Eissa et al, 2006;Fort et al, 2007).…”

“…However, structural modification was only observed when the reaction occurred in the presence of DTT (Eissa et al, 2006;Fort et al, 2007). Therefore the combination of a reducing agent and TG is a potential way of altering the antigenicity of b-Lg.…”

Heat‐Induced Gelation Mechanism of Blood Plasma Modulated by Cysteine

“…This pH dependence of thermal plasma gelation has to be considered as it can be added in meat products, typically acid pH. Studies focused on plasma heat‐induced gel properties improvement under acid pH utilizing microbial transglutaminase with or without Cys (0.25% w/v) as a reducing agent to unfold proteins have shown that although both contribute to get stronger gels, gel hardness was especially increased in the presence of Cys; however, Cys nullified the effects on its ability to retain water (Fort and others ).…”

Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

“…TG (EC 2.3.1.13) is an enzyme that catalyses acyl-transfer reactions between g-carboxyamide groups of glutamine residues and ε-amino group of lysine in proteins leading to inter-or intramolecular crosslinking (Jong & Koppelman, 2002;Kuraishi, Yamazaki, & Susa, 2001). bLactoglobulin is not a good substrate for TG; however, the reaction is facilitated after denaturation by heat treatment (>70 C) or by the addition of reducing agents such as dithiothreithol (DTT) or bmercaptoethanol, which cleave disulfide bonds (Aboumahmoud & Savello, 1990;Eissa, Puhl, Kadla, & Khan, 2006;Faergemand, Otte, & Qvist, 1997;Fort, Carretero, Parés, & Toldra, 2007). In a previous study Villas-Boas et al (2010) reported that b-Lg polymerized in the presence of cysteine (Cys), used as reducing agent, showed lower antigenic activity than that of the sample polymerized after thermal denaturation.…”