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Physico-Chemical Changes Induced by Gamma Irradiation on Some Structural Protein Extracts
Maria Stanca1, Carmen Gaidau1, Traian Zaharescu2
1Leather Research Department, Research and Development National Institute for Textiles and Leather-Division Leather and Footwear Research Institute, 93, Ion Minulescu Street, 031215 Bucharest, Romania.
Gamma irradiation affects protein stability differently, decreasing keratin
Area of Science:
- Biochemistry
- Materials Science
- Radiation Chemistry
Background:
- Proteins like keratin, collagen, and gelatin are vital biomaterials.
- Understanding their response to irradiation is crucial for applications in food, medicine, and industry.
- Gamma irradiation is a common method for material modification and sterilization.
Purpose of the Study:
- To investigate the impact of gamma irradiation (10 kGy) on the thermal and structural properties of keratin, collagen, and gelatin.
- To compare the effects of gamma irradiation with UV irradiation on protein secondary structure.
- To assess the influence of riboflavin on protein stability in both irradiated and non-irradiated samples.
Main Methods:
- Differential scanning calorimetry (μDSC) to assess thermal stability.
- Infrared (IR) spectroscopy to analyze changes in vibrational modes.
- Circular dichroism (CD) spectroscopy to evaluate secondary structure modifications.
- Electron paramagnetic resonance (EPR) spectroscopy to detect free radicals.
Main Results:
- Gamma irradiation decreased the thermal stability of keratin but increased the resistance to thermal denaturation in collagen and gelatins.
- Significant changes in protein secondary structure were observed after gamma irradiation, exceeding those from UV irradiation.
- Riboflavin exhibited a stabilizing effect on keratin and fish gelatin but a destabilizing effect on bovine gelatin.
- EPR spectroscopy confirmed the presence of oxygen-centered free radicals in gamma-irradiated samples, with signal enhancement over time in the presence of riboflavin.
Conclusions:
- Gamma irradiation differentially impacts the thermal stability and structural integrity of keratin, collagen, and gelatin.
- The findings highlight the potential for targeted modification of protein properties using gamma irradiation.
- Riboflavin can modulate the effects of irradiation on protein structure, suggesting its role in radioprotection or radiosensitization.
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