ArticleMolecules (Basel, Switzerland)2021
Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics.
Article in Molecules (Basel, Switzerland), 2021. 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.
- Article
- Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure.Foods (Basel, Switzerland) · 2025Article
- Casein-Based Biomaterials: Fabrication and Wound Healing Applications.Molecules (Basel, Switzerland) · 2025Review
- Investigation of the structural, functional, and digestive properties of beta-casein from cow, goat, and donkey milk.Food chemistry: X · 2025Article
- Casein-based film enriched with lignin as a biodegradable substrate for enzyme immobilization.RSC advances · 2025Article
- Impact of Reconstitution Conditions on the Solubility of Faba Bean Protein Isolate.Foods (Basel, Switzerland) · 2024Article
- The Impact of Varying Lactose-to-Maltodextrin Ratios on the Physicochemical and Structural Characteristics of Pasteurized and Concentrated Skim and Whole Milk-Tea Blends.Foods (Basel, Switzerland) · 2024Article
- Health-Related Outcomes and Molecular Methods for the Characterization of A1 and A2 Cow's Milk: Review and Update.Veterinary sciences · 2024Review
- Structural Properties of Casein Micelles with Adjusted Micellar Calcium Phosphate Content.Foods (Basel, Switzerland) · 2024Article
- Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity.International journal of food science · 2024Article
- Feature Papers in Food Chemistry.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
4 authors.
Funding
Abstract
This study investigated structural changes in β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH had strongly affected the secondary structure of β-casein, with most affected regions involving random coils and α-helical structures. The α-helical structures showed great pH sensitivity by decreasing at 20 °C and diminishing completely at 4 °C when pH was increased from 5.9 to 7.0. The decrease in α-helix was likely related to the greater presence of random coils at pH 7.0, which was not observed at pH 5.9 at either temperature. The changes in secondary structure components were linked to decreased hydrophobic interactions at lower temperature and increasing pH. The most prominent change of the α-helix took place when the pH was adjusted to 7.0 and the temperature set at 4 °C, which confirms the disruption of the hydrogen bonds and weakening of hydrophobic interactions in the system. The findings can assist in establishing the structural behaviour of the β-casein under conditions that apply as important for solubility and production of β-casein.
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