Effect of enzymatic glycosylation on the structure and properties of wheat gluten protein fibers

Abstract

Wheat gluten proteins are good raw materials for preparing fibers due to their excellent viscoelasticity. However, protein fibers made directly from wheat gluten have poor mechanical properties. In this paper, transglutaminase was used to induce the glycosylation reaction between wheat gluten proteins and carboxymethyl chitosan. The glycated proteins were then made into fibers by wet spinning. After glycosylation modification, the breaking strength and breaking elongation of the wheat gluten protein fibers (WGPF) improved by 43% and 127%, respectively. Fourier transform infrared spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses revealed that the glycosylation-modified WGPF molecules contained saccharide portions, which confirms the covalent attachment of carboxymethyl chitosan to the wheat gluten protein. Scanning electron microscopy showed that the number of pores in the cross-section of the modified WGPF was lower than that in the unmodified WGPF. The thermal stability and dyeability of the modified WGPF were also improved.

Comparison of the Effects of pH-Shifting, Acetic Acid Modification, and TGase Treatment on the Physicochemical and Functional Properties of Wheat Gluten Protein

“…The pH group showed broader absorption peak in the 3,600-3,300 cm − 1 regions, indicating higher levels of -OH and -NH 2 groups. According to previous studies (Lei & Ma, 2021), all treatment groups showed a more pronounced absorption peak at 2,364 cm − 1 , which was attributed to NH 2 stretching vibrations. The absorption peak of the control group was much sharper, resulting that WGP had a high denaturation temperature (Fig.…”

“…Enzymatic treatment (ET): The ET was based on the method of Lei et al with minor modi cations (Lei, & Ma, 2021). The 1% WGP (W/V) was dissolved in deionized water stirred for 0.5 h, after adding 20 U/g of TGase (transglutaminase), the solution was placed in a water bath (40°C) and shaked at 110 r/min for 24 h. After that, the suspension was cooled in an ice-water bath to inhibit enzyme activity.…”

Exploring the Role of Lactoferrin in Managing Allergic Airway Diseases among Children: Unrevealing a Potential Breakthrough

“…Heating to 121 °C denatured all LF in both milk samples within 4 s [ 176 ]. Additionally, it has been reported that a protein’s glycosylation patterns may influence its thermal stability [ 177 ]. Specifically, in the case of LF, glycosylation at Asn281 shields bovine lactoferrin from trypsin cleavage at Lys282, whereas the glycosylation of human lactoferrin does not offer similar protection [ 178 ].…”

A Review of the Mechanism, Properties, and Applications of Hydrogels Prepared by Enzymatic Cross-linking

“…These films could be significantly improved, serving as potential candidates for high-watercontent food packaging. 119 The addition of TGase to whey protein-polycarboxymethyl chitosan to prepare composite membranes greatly improved the stretching of plastics and could potentially prevent environmental pollution problems. TGase markedly promoted the stretching ability of WPC plastics, with elongation increasing from 7.3% to 31.3% due to TGase treatment.…”

“…TGase and zinc have been used to prepare gelatin hydrogel films, which were insoluble and permeable, with suitable mechanical properties. These films could be significantly improved, serving as potential candidates for high-water-content food packaging . The addition of TGase to whey protein-poly­carboxy­methyl chitosan to prepare composite membranes greatly improved the stretching of plastics and could potentially prevent environmental pollution problems.…”