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Impact of a protease and xylanase cocktail on the physicochemical properties of wafer batter and sheets

Sadeghian-Motahar, S. F., Rodriguez Garcia, J., Tosi, P. ORCID: https://orcid.org/0000-0003-4171-6120, Kuschel, B., Merz, M., Osborne, J. and Chatzifragkou, A. ORCID: https://orcid.org/0000-0002-9255-7871 (2025) Impact of a protease and xylanase cocktail on the physicochemical properties of wafer batter and sheets. Future Foods, 12. 100830. ISSN 2666-8335

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To link to this item DOI: 10.1016/j.fufo.2025.100830

Abstract/Summary

This study investigated enzymatic treatment as a mean of regulating viscosity in wheat flour batter and its impact on the quality of wafer sheets. Parameters such as enzyme concentration and hydrolysis time were evaluated. Changes in the secondary structures of proteins in flour and commercial gluten were further investigated using attenuated total reflectance-fourier transform infrared spectroscopy (ATR-FTIR), confirming a decrease in α-helix and β-sheet structures. Enzymatic hydrolysis of gluten led to the unfolding of protein structure, resulting in an increase in free sulfhydryl group content. Rheological analysis of batters revealed a decrease in apparent viscosity in enzymatically treated batters compared to control ones. Enzymatic proteolysis caused a decrease in both storage modulus (G′) and loss modulus (G″) compared to control, indicating a weakened elastic structure and a more liquid-like behaviour. Enzyme-treated wafer sheets showed lower hardness and fracturability compared to control ones. These findings suggest that proteolytic enzymes could alter the chemical structure of gluten and the rheological properties of wafer batter leading to a reduction in batter viscosity, structural protein matrix, and the production of softer wafer sheets

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Agriculture, Policy and Development > Department of Crop Science
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
ID Code:125506
Publisher:Elsevier

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