ArticleMolecules (Basel, Switzerland)2017
Structural and Functional Properties Changes of β-Conglycinin Exposed to Hydroxyl Radical-Generating Systems.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
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- The Impact of AAPH-Induced Oxidation on the Functional and Structural Properties, and Proteomics of Arachin.Molecules (Basel, Switzerland) · 2023Article
- Esterified Soy Proteins with Enhanced Antibacterial Properties for the Stabilization of Nano-Emulsions under Acidic Conditions.Molecules (Basel, Switzerland) · 2023Article
- Ultrasound-Assisted Extraction of Protein fromMolecules (Basel, Switzerland) · 2023Article
- Impact of Cavitation Jet on the Structural, Emulsifying Features and Interfacial Features of Soluble Soybean Protein Oxidized Aggregates.Foods (Basel, Switzerland) · 2023Article
- The temporal evolution mechanism of structure and function of oxidized soy protein aggregates.Food chemistry: X · 2022Article
- Effect of Peroxyl Radical-Induced Oxidation on Functional and Structural Characteristics of Walnut Protein Isolates Revealed by High-Resolution Mass Spectrometry.Foods (Basel, Switzerland) · 2022Article
- Animal and Plant Protein Oxidation: Chemical and Functional Property Significance.Foods (Basel, Switzerland) · 2020Review
- The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage.Molecules (Basel, Switzerland) · 2018Article
- Molecular and Functional Properties of Protein Fractions and Isolate from Cashew Nut (Anacardium occidentale L.).Molecules (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The objective of the present study was to examine the structural and functional changes of β-conglycinin exposed to oxidizing radicals produced by FeCl₃/H₂O₂/ascorbic acid hydroxyl radical-generating system (HRGS) for 3 h at room temperature. Increasing H₂O₂ concentrations resulted in a loss of histidine residues, lysine residues, and available lysine, which was accompanied by the formation of protein carbonyls and disulphide bonds (
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