Keywords

Wheat Gluten Composite Modification Characteristics Structure Wheat Gluten Composite Modification Characteristics Structure

Abstract

This paper studied the changes in rheological and thermal properties of wheat gluten protein (WG) after trypsin restriction enzymatic hydrolysis and transglutaminase (TG enzyme) cross-linking, and characterized the structure of wheat gluten protein. The results show that appropriate trypsin restriction enzymatic hydrolysis is beneficial to the cross-linking effect of TG enzyme on wheat gluten protein. The use of 80 U/g trypsin restriction enzymatic hydrolysis and TG enzyme cross-linking compound modification effect is the most significant, and its elastic modulus The quantity G’ and thermal denaturation temperature Tg increased from 2.26 kPa and 55.59 ¡æ to 6.46 kPa and 59.17 ¡æ respectively. Structural analysis of wheat gluten protein shows that appropriate trypsin restriction enzymatic hydrolysis can break the disulfide bonds between wheat gluten protein molecules and increase surface hydrophobicity, thus making the tight wheat gluten protein structure looser and exposed. More glutamine residues are released for TG enzyme cross-linking, resulting in the hydrated wheat gluten protein forming a more porous and dense wheat gluten protein network structure. However, excessive enzymatic hydrolysis will be detrimental to the cross-linking reaction of TG enzyme. Changes in the rheological behavior and thermal properties of wheat gluten after trypsin-based enzymatic hydrolysis and the subsequent transglutaminase (TGase) catalyzed cross-linking reactions were investigated and the structure of wheat gluten was characterized. The results indicate that an appropriate degree of trypsin- based partial enzymatic hydrolysis favored TGase cross-linking. The most significant composite modification effect was observed when 80 U/g trypsin-based partial hydrolysis was combined with TGase cross-linking, where the wheat gluten storage modulus (G’) and thermal denaturation temperature (Tg) increased from 2.26 kPa and 55.59¡ãC to 6.46 kPa and 59.17¡ãC, respectively. Structural analysis indicated that an appropriate degree of trypsin-based enzymatic hydrolysis could result in breakage of intermolecular disulfide bonds and an increase in surface hydrophobicity. Consequently , the compact wheat gluten structure became loose and more glutamine residues were exposed to allow TGase cross-linking. This resulted in the formation of a more compact and porous wheat gluten network structure from the hydrated wheat gluten. However, excessive enzymatic hydrolysis was unsuitable for TGase cross-linking.

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Original research done by Wang Kaiqiang

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