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Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
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Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
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Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure

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Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
Journal Article

Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure

2025
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Overview
This study explored the functionalization of sodium caseinate (NaCas) using environmentally friendly approaches to improve the mechanical and structural properties of the derived films. NaCas functionalization was achieved through casein crosslinking using two approaches: (i) thermal treatment at an alkaline pH to induce the formation of lysinoalanine (LAL) and (ii) riboflavin-mediated photo-oxidation to induce the formation of di-tyrosine (di-Tyr). Starting from NaCas (not functionalized, control) obtained from pasteurized milk, three functionalized NaCas samples were prepared: one sample crosslinked by LAL, and two samples crosslinked by di-Tyr formed under LED light either with or without riboflavin. The amount of crosslinking was evaluated in the acid hydrolysates through HPLC methods using either fluorescence (di-Tyr) or MS (LAL) detection. Heat treatment at pH 9 induced the formation of up to 3540 µg of LAL/g casein, whereas LED light exposure in the presence of riboflavin promoted the formation of up to 500 µg of di-Tyr/g casein. The formation of crosslinks at the intermolecular level, which resulted in protein aggregation, was detected by SDS-PAGE. Films were obtained by mixing the water solutions of the four NaCas samples with glycerol as the plasticizer and casting them. The FTIR spectra revealed that the formation of crosslinks also induced changes in the secondary structure of NaCas, which were conserved in the derived films. Mechanical testing demonstrated that di-Tyr crosslinks enhanced film ductility, while LAL crosslinks increased tensile strength and stiffness.