Extraction and characterization of collagen to develop biopolymeric fiber from chicken feet.
Call Number: AIT Thesis no.FB-15-09 Material type:
SeriesSeries: Asian Institute of Technology. Thesis ; no. no.FB-15-09Publication details: Pathum Thani, Thailand : Asian Institute of Technology, 2015Description: 83 leaves : ill. + 1 online resourceSubject(s): Online resources: Dissertation note: Thesis (M. Sc.) - Asian Institute of Technology, 2015 Summary: Collagen was extracted sequencially from the chicken feet using papain, acetic acid and NaCl solution. The optimum condition was found to be 30 ⁰ C temperature treatment and ( 25 ml/mg ) 0.9N NaCl concentration . The incubation time has not significant effect on yield of collagen . The highest yield ( 32.16% ) was found by the enzymatic hydrolysis for 28hr at 30 ⁰ C and (25ml /mg) of 0.9 N NaCl concentration. At lower temperature (4 ⁰ C) of incubation, the yields were less. The molecular weight of 150kDa and 250kDa and absorbance at 220 -230nm of collagen indicates 99% purity . The FTIR shows the presence of native structure of collagen. The linear decreasing trend in the relative viscosity of chicken feet collagen was seen with the increased temperature. Scanning Electron Microscopy ( SEM ) reveals the interconnected network of porous structure of collagen. The slight shifting of all the peaks of FTIR is the concrete evidence of interactions that occurs between the Polycapralactone (PCL) and the collagen. The Minimum Inhibitory Concentration ( MIC ) for Ag -PCL -collagen nanofibers was found to be 0.5 mm at 10 mg/ml for Ecsherichia coli and 0.5 mm at 20 mg/ml for Salmonella typhimurium . The combination of silver -collagen -Polycapralactone fibers could be used as a bio packaging materials.
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A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in Food Engineering and Bioprocess Technology, School of Environment, Resources and Development
Thesis (M. Sc.) - Asian Institute of Technology, 2015
Collagen was extracted sequencially from the chicken feet using papain, acetic acid and NaCl solution. The optimum condition was found to be 30 ⁰ C temperature treatment and ( 25 ml/mg ) 0.9N NaCl concentration . The incubation time has not significant effect on yield of collagen . The highest yield ( 32.16% ) was found by the enzymatic hydrolysis for 28hr at 30 ⁰ C and (25ml /mg) of 0.9 N NaCl concentration. At lower temperature (4 ⁰ C) of incubation, the yields were less. The molecular weight of 150kDa and 250kDa and absorbance at 220 -230nm of collagen indicates 99% purity . The FTIR shows the presence of native structure of collagen. The linear decreasing trend in the relative viscosity of chicken feet collagen was seen with the increased temperature. Scanning Electron Microscopy ( SEM ) reveals the interconnected network of porous structure of collagen. The slight shifting of all the peaks of FTIR is the concrete evidence of interactions that occurs between the Polycapralactone (PCL) and the collagen. The Minimum Inhibitory Concentration ( MIC ) for Ag -PCL -collagen nanofibers was found to be 0.5 mm at 10 mg/ml for Ecsherichia coli and 0.5 mm at 20 mg/ml for Salmonella typhimurium . The combination of silver -collagen -Polycapralactone fibers could be used as a bio packaging materials.
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