Physical properties of zein networks treated with microbial transglutaminase

Potential improvements to the physical properties of brittle, self-assembled zein networks through microbial transglutaminase crosslinking were investigated. The formation of crosslinked heteropolymers was also explored with networks containing zein and either soy or pea protein isolates as supplemented lysine sources. The observed SDS-PAGE bands did not show any evidence of zein crosslinking. Soy and pea isolates underwent extensive crosslinking on their own, but heteropolymers were not observed in multiprotein networks with zein. Despite the lack of crosslinking observed, rheological and textural analysis revealed that the enzymatic treatment of zein produced a weaker, more brittle structure. With no significant changes in secondary structure, determined through FTIR, the observed behaviour was primarily attributed to glutamine deamidation by microbial transglutaminase in the absence of sufficient lysine through changes to the hydrophobicity of the protein such that non-covalent bonding within network was modified.

Automated summary

This study investigated potential improvements to the physical properties of brittle, self-assembled zein networks through microbial transglutaminase crosslinking. Although crosslinked heteropolymers were observed, they were not found in multiprotein networks with zein, resulting in a weaker structure. The observed behavior was mainly attributed to glutamine deamidation by microbial transglutaminase, changing the hydrophobicity of the protein and modifying non-covalent bonding within the network.