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ARS Home » Northeast Area » Beltsville, Maryland (BARC) » Beltsville Agricultural Research Center » Food Quality Laboratory » Research » Publications at this Location » Publication #385355
Research Project: Integrated Approaches to Improve Fruit and Vegetable Nutritional Quality with Improved Phenolics Contents

Location: Food Quality Laboratory

Title: Heat mediated physicochemical and structural changes of wheat gluten in the presence of salt and alkali

Author
item HAN, CHUANWU - Qingdao Agricultural University
item MA, MENG - Qingdao Agricultural University
item Yang, Tianbao
item LI, MAN - Qingdao Agricultural University
item SUN, QINGJIE - Qingdao Agricultural University

Submitted to: Food Hydrocolloids
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/19/2021
Publication Date: 11/20/2021
Citation: Han, C., Ma, M., Yang, T., Li, M., Sun, Q. 2021. Heat mediated physicochemical and structural changes of wheat gluten in the presence of salt and alkali. Journal of Agricultural and Food Chemistry. 120:106971. https://doi.org/10.1016/j.foodhyd.2021.106971.
DOI: https://doi.org/10.1016/j.foodhyd.2021.106971

Interpretive Summary: Gluten is a family of proteins in wheat flour to affect the dough extensibility and quality of wheat product. The objective of this study was to understand the heat mediated cross-linking mechanism of gluten in the presence of salt and alkali. The G' value (measurement of extensibility) of gluten was mediated by heating, while alkali delayed the transition temperature by approximately 20 °C. Salt increased the extensibility of gluten. However, alkali improved gluten strength and toughness. Hydrophobic interactions and aggregations of protein molecular chains were enhanced by both salt and alkali, and heating further promoted these interactions. In addition, alkali reduced the aggregation temperature of large glutenin polymers from 95 to 75 °C. RP-HPLC patterns confirmed that a- and '- gliadin subunits were more susceptible to heat and polymerized after heating at 95 °C with alkali. Alkali promoted protein-protein interactions in gluten, which was positively correlated with temperature. This study provides a more comprehensive theoretical basis for the control of gluten properties and quality of wheat products.

Technical Abstract: Gluten is a family of proteins in wheat flour to affect the dough extensibility and quality of wheat product. The objective of this study was to understand the heat mediated cross-linking mechanism of gluten in the presence of salt and alkali. The G' value of gluten was mediated by heating, while alkali delayed the transition temperature by approximately 20 °C. Salt increased the extensibility of gluten. However, alkali improved gluten strength and toughness. Fluorescence spectroscopy, surface hydrophobicity, and AFM images demonstrated that hydrophobic interactions and aggregations of protein molecular chains were enhanced by both salt and alkali, and heating further promoted these interactions. In addition, alkali reduced the aggregation temperature of large glutenin polymers from 95 to 75 °C according to SE-HPLC profiles. RP-HPLC patterns confirmed that a- and '- gliadin subunits were more susceptible to heat and polymerized after heating at 95 °C with alkali. QCM-D results showed that alkali promoted protein-protein interactions in gluten, which was positively correlated with temperature. This study provides a more comprehensive theoretical basis for the control of gluten properties and quality of wheat products.