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Optimization of collagen extraction from chicken feet by papain hydrolysis and synthesis of chicken feet collagen based biopolymeric fibres
The extraction of collagen from chicken feet by papain hydrolysis was optimized at various temperatures, time and solid to solvent ratios. The optimum extraction condition (with highest yield, 32.16%, w/w) was found after 28 h of enzymatic hydrolysis at 30 ⁰C. The chicken feet collagen was found ric...
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Published in: | Food bioscience 2018-06, Vol.23, p.23-30 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The extraction of collagen from chicken feet by papain hydrolysis was optimized at various temperatures, time and solid to solvent ratios. The optimum extraction condition (with highest yield, 32.16%, w/w) was found after 28 h of enzymatic hydrolysis at 30 ⁰C. The chicken feet collagen was found rich in glycine (16.30%), hydroxyproline (14.15%) and proline (8.70%). The molecular weight distribution of isolated collagen was found in the range of 25–150 kDa. The functional characteristics of chicken feet collagen such as solubility, emulsification, foaming, water and oil holding capacity indicate its potential application in food, pharmaceuticals and cosmetics products. The fibres were also developed by electrospinning from chicken feet extracted collagen and polycaprolactone. Scanning electron micrographs demonstrated the interconnected network of porous structure of collagen and its bio-polymeric fibres. The slight shifting and sharp absorption of peaks obtained from biopolymeric collagen presented the evidence of interactions, occurred between the polycapralactone and the collagen.
•The valorisation of chicken feet for optimized extraction of collagen.•The evaluation of amino acid profile and functional properties of chicken feet collagen.•The development and characterization of chicken feet collagen based biopolymeric fibres. |
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ISSN: | 2212-4292 2212-4306 |
DOI: | 10.1016/j.fbio.2018.03.003 |