ArticleFrontiers in nutrition2021
Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics.
Article in Frontiers in nutrition, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 18 citations in OpenAlex.
- Evaluation of the Functional Properties and Edible Safety of Concocted Xanthii Fructus Protein.Foods (Basel, Switzerland) · 2025Article
- A Novel Variable Selection Method Based on Binning-Normalized Mutual Information for Multivariate Calibration.Molecules (Basel, Switzerland) · 2023Article
- Water as a Probe for Standardization of Near-Infrared Spectra by Mutual-Individual Factor Analysis.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peanut allergy is becoming a life-threatening disease that could induce severe allergic reactions in modern society, especially for children. The most promising method applied for deallergization is heating pretreatment. However, the mechanism from the view of spectroscopy has not been illustrated. In this study, near-infrared spectroscopy (NIRS) combined with aquaphotomics was introduced to help us understand the detailed structural changes information during the heating process. First, near-infrared (NIR) spectra of Ara h1 were acquired from 25 to 80°C. Then, aquaphotomics processing tools including principal component analysis (PCA), continuous wavelet transform (CWT), and two-dimensional correlation spectroscopy (2D-COS) were utilized for better understanding the thermodynamic changes, secondary structure, and the hydrogen bond network of Ara h1. The results indicated that about 55°C could be a key temperature, which was the structural change point. During the heating process, the hydrogen bond network was destroyed, free water was increased, and the content of protein secondary structure was changed. Moreover, it could reveal the interaction between the water structure and Ara h1 from the perspective of water molecules, and explain the effect of temperature on the Ara h1 structure and hydrogen-bonding system. Thus, this study described a new way to explore the thermodynamic properties of Ara h1 from the perspective of spectroscopy and laid a theoretical foundation for the application of temperature-desensitized protein products.
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