Development of biodegradable films from whey proteins by cross-linking and entrapment in cellulose
| Autor: | C. Le Tien, G. Delmas-Patterson, H L Yu, Pompilia Ispas-Szabo, M Letendre, Monique Lacroix, Mircea-Alexandru Mateescu |
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| Rok vydání: | 2000 |
| Předmět: |
Whey protein
food.ingredient Hot Temperature Size-exclusion chromatography engineering.material Gelatin chemistry.chemical_compound food Protein structure Cellulose Chromatography Molecular mass Proteolytic enzymes General Chemistry Milk Proteins Biodegradation Environmental Cross-Linking Reagents Whey Proteins chemistry Gamma Rays engineering Biophysics Thermodynamics Biopolymer General Agricultural and Biological Sciences Rheology |
| Zdroj: | Journal of agricultural and food chemistry. 48(11) |
| ISSN: | 0021-8561 |
| Popis: | When cross-linked by heating or by gamma-irradiation and entrapped in cellulose, whey proteins can generate insoluble biofilms with good mechanical properties and high resistance to attack by proteolytic enzymes. Interchain cross-linking of proteins generated an increase in the puncture strength, and a decrease in water vapor permeability. Gelatin was added in film formulation as a stabilizer to improve the puncture strength and film appearance. The structure of the biofilms was also analyzed. SDS-PAGE revealed that heating and gamma-irradiation produce an increase of the molecular weight of the cross-linked protein. Size exclusion chromatography showed a molecular mass of 40 kDa for un-cross-linked whey proteins, whereas for the soluble fractions of the cross-linked proteins, molecular distributions were between 600 and 3800 kDa for the heated proteins and between 1000 and 2000 kDa for gamma-irradiated proteins. No major alteration of the structural conformation of the proteins was observed by FTIR for biofilms obtained after heat treatment, whereas gamma-irradiation induced some modifications in the protein structure. X-ray diffraction analysis suggests that cross-linking by gamma-irradiation seems to modify the conformation of proteins, which became more ordered and more stable. |
| Databáze: | OpenAIRE |
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