碩士 / 國立成功大學 / 化學系碩博士班 / 98 / The aim of the study was to investigate the extraction conditions of collagen extracted from Taiwan tilapia scale and the analysis of its physical-chemical properties. Experiment result shows that add few pepsin in HCl extraction solution (pH 2) could highly increase the production rate of collagen. The identify of physical-chemical properties includes using amino acid analysis, circular dichroism (CD), sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE) and differential scanning calorimetry (DSC) to determine the amino acid composition, secondary structure changing with denaturation, denature temperature (Td) and molecular weight. Amino acid analysis indicates that Taiwan tilapia scale collagen contains 11.23% hydroxyproline. SDS-PAGE electrophoresis result shows this collagen was mainly composed of α1, α2 monomer, β dimer and γ trimer, which is related to type I collagen, and no polypeptides bands below 50 kDa represent that Telopeptide was removed during extraction process.
The dehydrothermal treatment (DHT) stable the collagen structure, which can increase the denature temperature (Td). The scanning electron microscope (SEM) is to observe and compare the surface structure changing, and ninhydrin (NHN) assay results showed that DHT at125 ℃ the cross-linking index was 31.34%; it was 55.97% for DHT at 150 ℃. The cross-linking of collagen has the characteristics of high intensity and high stability. In application, it can promote mechanical strength of biomaterials and can resist immune system and enzyme attack in human body.
| Identifer | oai:union.ndltd.org:TW/098NCKU5065088 |
| Date | January 2010 |
| Creators | Ar-Chinghsieh, 謝雅青 |
| Contributors | Fu-Yung Huang, 黃福永 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 77 |
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