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Effect of Heat Treatment on Gelatin Properties of Pepsin-Soluble Collagen from Chicken Bones
- Source :
- Current Topics in Nutraceutical Research. 18:1-9
- Publication Year :
- 2018
- Publisher :
- New Century Health Publishers LLC, 2018.
-
Abstract
- The aim of this study was to evaluate the physicochemical composition and gelatin properties of collagen hydrolysates obtained from chicken bones under different heat treatment temperatures (50, 70 and 90°C) and times (30, 60 and 90 min). Results showed that heat temperature can significantly improve the solubility of protein (from 37.8 to 72.1%). Degree of hydrolysis and SDS-PAGE analysis showed that the mean molecular weight of collagen hydrolysates at 50 and 70°C were higher than that of hydrolysates at 90°C, which indicating that the triple-helix structure of protein transmitted to chains and subsequently form protein-protein linkages during heating. FTIR analysis demonstrated that the relative content of β-sheet decreased and random coil increased significantly (P < 0.05), whereas α-helix and β-turn had no significant changes during heating treatment (P > 0.05). Collagen hydrolysates obtained at 90°C for 30 min indicated better gelatin properties (melting temperature, texture profile analysis and microstructure) when compared with that of hydrolysates obtained at 50 and 70°C. Therefore, heat treatment with a relatively higher temperature (90°C) and shorter time (30 min) is necessary to obtain hydrolyzed chicken bones collagen with good gelatin properties.
Details
- ISSN :
- 15407535
- Volume :
- 18
- Database :
- OpenAIRE
- Journal :
- Current Topics in Nutraceutical Research
- Accession number :
- edsair.doi...........e71223af64671799cd3321519a2f7c1f