Extraction Of Collagen From Quail (Coturnix Japonica) Feet: Characterization And Development Of Electrospun Nanofibers
Poultry processing plants produce a huge amount of wastes. The discharge of these amounts of wastes has raised serious concerns regarding their environmental impacts, diseases, and loss of valuable biological resources like proteins and lipids. Utilization of these by-products for producing value...
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| Main Author: | |
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| Format: | Thesis |
| Language: | English |
| Published: |
2019
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| Subjects: | |
| Online Access: | http://eprints.usm.my/48591/1/Mahsa_EXTRACTION%20OF%20COLLAGEN%20FROM%20QUAIL%20cut.pdf http://eprints.usm.my/48591/ |
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| Institution: | Universiti Sains Malaysia |
| Language: | English |
| Summary: | Poultry processing plants produce a huge amount of wastes. The discharge of these
amounts of wastes has raised serious concerns regarding their environmental impacts,
diseases, and loss of valuable biological resources like proteins and lipids. Utilization
of these by-products for producing value-added products may offer a feasible and economically
viable solution. This line of thought led to the research on the by-products
as sources of collagen. In this study, quails’ feet from poultry processing by-products
was utilized as a new source of collagen along with other applications such as electrospun
nanofibers. In this way, acid and pepsin soluble collagens and also lactic acid
and lactic acid pepsin soluble collagens were extracted from quails’ feet and characterized.
The physicochemical, thermal and morphological properties of the extracted
collagens are investigated. The electrophoretic patterns indicated that all samples were
type-I collagen with three different chains. Amino acid analysis demonstrated that the
imino acid contents of the samples are higher than those of calf-skin, pig-skin, and
chicken feet collagens. The FTIR spectra suggested that the extracted collagens were
in triple-helical structure. The zeta-potential analysis is shown the isoelectric points
of the collagens are in the pH range of 5.24-5.61. Differential scanning calorimetry
and thermogravimetric analyses indicated that the extracted collagens had higher thermal
stability in comparison to calf-skin and pig-skin collagens. The result showed that
the correlation between the thermal stability of collagen and the imino acid content. |
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