Effects of partial hydrolysis and subsequent cross-linking on wheat gluten physicochemical properties and structure

•An appropriate hydrolysis allowed the compact wheat gluten structure to unfold.•The unfold structure facilitates MTGase cross-linking.•Composite modification could improve wheat gluten rheological behavior and thermal properties.•Excessive hydrolysis resulted in HMW-GS degrading to smaller peptides...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Food chemistry 2016-04, Vol.197 (Pt A), p.168-174
Hauptverfasser: Wang, Kaiqiang, Luo, Shuizhong, Cai, Jing, Sun, Qiaoqiao, Zhao, Yanyan, Zhong, Xiyang, Jiang, Shaotong, Zheng, Zhi
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:•An appropriate hydrolysis allowed the compact wheat gluten structure to unfold.•The unfold structure facilitates MTGase cross-linking.•Composite modification could improve wheat gluten rheological behavior and thermal properties.•Excessive hydrolysis resulted in HMW-GS degrading to smaller peptides. The rheological behavior and thermal properties of wheat gluten following partial hydrolysis using Alcalase and subsequent microbial transglutaminase (MTGase) cross-linking were investigated. The wheat gluten storage modulus (G′) and thermal denaturation temperature (Tg) were significantly increased from 2.26kPa and 54.43°C to 7.76kPa and 57.69°C, respectively, by the combined action of partial hydrolysis (DH 0.187%) and cross-linking. The free SH content, surface hydrophobicity, and secondary structure analysis suggested that an appropriate degree of Alcalase-based hydrolysis allowed the compact wheat gluten structure to unfold, increasing the β-sheet content and surface hydrophobicity. This improved its molecular flexibility and exposed additional glutamine sites for MTGase cross-linking. SEM images showed that a compact 3D network formed, while SDS–PAGE profiles revealed that excessive hydrolysis resulted in high-molecular-weight subunits degrading to smaller peptides, unsuitable for cross-linking. It was also demonstrated that the combination of Alcalase-based partial hydrolysis with MTGase cross-linking might be an effective method for modifying wheat gluten rheological behavior and thermal properties.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2015.10.123