ArticleInternational journal of molecular sciences2023
Degree of Hydrolysis Regulated by Enzyme Mediation of Wheat Gluten Fibrillation: Structural Characterization and Analysis of the Mechanism of Action.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 17 citations in OpenAlex.
- Unveiling the patterns and mechanisms of time-specific release of multifunctional peptides from cricket protein.Food chemistry: X · 2026Article
- Optimization of Enzymatic Hydrolysis by Protease Produced fromInternational journal of food science · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The impact of different degrees of hydrolysis (DHs) on fibrillation when trypsin mediates wheat gluten (WG) fibrillation has not been thoroughly investigated. This study discussed the differences in amyloid fibrils (AFs) formed from wheat gluten peptides (WGPs) at various DH values. The results from Thioflavin T (ThT) fluorescence analysis indicated that WGPs with DH6 were able to form the most AFs. Changes in Fourier Transform Infrared (FTIR) absorption spectra and secondary structure also suggested a higher degree of fibrillation in DH6 WGPs. Analysis of surface hydrophobicity and ζ-potential showed that DH6 AFs had the highest surface hydrophobicity and the most stable water solutions. Scanning Electron Microscopy (SEM) and Transmission Electron Microscopy (TEM) images revealed the best overall morphology of DH6 AFs. These findings can offer valuable insights into the development of a standardized method for preparing wheat gluten amyloid fibrils.
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