Stability of the Meat Protein Type I Collagen: Influence of pH, Ionic Strength, and Phenolic Antioxidant
| Autor: | Antonello Santini, Maurizio Delfini, Fabio Sciubba, Massimo Lucarini, Alessandra Durazzo, Raffaella Gianferri, Ginevra Lombardi-Boccia, Maria Enrica Di Cocco, Mosè Alise |
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| Přispěvatelé: | Lucarini, Massimo, Durazzo, Alessandra, Sciubba, Fabio, Enrica Di Cocco, Maria, Gianferri, Raffaella, Alise, Mosè, Santini, Antonello, Delfini, Maurizio, Lombardi-Boccia, Ginevra |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
collagen
Health (social science) Plant Science lcsh:Chemical technology 01 natural sciences Health Professions (miscellaneous) Microbiology chemistry.chemical_compound meat 1H NMR H NMR Catechin Collagen Ionic strength Meat PH T2 relaxation 0404 agricultural biotechnology catechin Molecule lcsh:TP1-1185 Water diffusion Phenolic antioxidant pH Communication 010401 analytical chemistry 04 agricultural and veterinary sciences 040401 food science 0104 chemical sciences chemistry Proton NMR Biophysics ionic strength Type I collagen Function (biology) Food Science |
| Zdroj: | Foods, Vol 9, Iss 480, p 480 (2020) Foods |
| ISSN: | 2304-8158 |
| Popis: | The water-holding capacity (WHC) is among the key factors in determining the quality of meat and its value, which is strongly influenced by the content and quality of the connective tissue proteins like collagen. Therefore, the factors that influence the proteins’ stability, e.g., pH, ionic strength, and the antioxidants which are used to increase the meat shelf-life, also affect the WHC. The interaction of collagen, whose structure is strongly influenced by the interaction with water molecules, can be studied following the behavior of water diffusion by low-resolution 1H NMR experiments. The present study is addressed to study the collagen stability as a function of pH, ionic strength, and phenolic antioxidants like catechin. The experimental study demonstrated how the 1H NMR time domain (TD) experiments are able to evaluate the hydration properties of collagen, not only as a function of ionic strength and pH, but also in determining the ability of catechin to interact both on the surface of the collagen fibrils and inside the fibrillar domain. |
| Databáze: | OpenAIRE |
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