The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia
碩士 === 國立成功大學 === 化學系碩博士班 === 98 === This study was to investigate the extraction methods and the characterization of fish scale collagen from Taiwan Tilapia. The main objective was to focus on the cross-linkage with ribose and to characterize the thermal stability of this cross-linked collagen/ribo...
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ndltd-TW-098NCKU50650902015-11-06T04:03:47Z http://ndltd.ncl.edu.tw/handle/25182854271636957546 The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia 台灣鯛魚鱗膠原蛋白核糖交聯之研究 Chien-ChihLin 林建智 碩士 國立成功大學 化學系碩博士班 98 This study was to investigate the extraction methods and the characterization of fish scale collagen from Taiwan Tilapia. The main objective was to focus on the cross-linkage with ribose and to characterize the thermal stability of this cross-linked collagen/ribose film. It was found that the extraction rate is dependent on the concentration of pepsin and extraction time. The optimum condition was as of in pH 2 aqueous solution, extraction time over 24 hours and catalyzed by pepsin with a concentration of mg/mL. The collagen thus extracted was characterized by using Hydroxyproline quantification method, UV and FT-IR spectroscopy, viscometer, differential scanning calorimetry (DSC), Circular Dichroism Spectroscopy (CD), scanning electronic microscope (SEM). The results showed that the concentration of the extracted collagen is 0.937 mg/mL. The band at 230 nm (Histidine) of UV spectrum, the bands at 1661 cm-1, 1546 cm-1, 1239 cm-1of IR spectrum, and the positive band at 223 nm and negative band at 202 nm (triple helix structure) analyzed by CD are the collagen characteristic. The Td of solution in the concentration of (0.3mg/ml) was 33 oC. The Td of lyophilized collagen analyzed by DSC was 73 oC. The optimum cross-linking condition was that the concentration ratio of collagen to ribose is 2mg/ml to 0.2 M and the cross-linking time is 8 hours. The FT-IR spectrum of the cross-linked film showed the coexistence of collogen and ribose.The Td of the cross-linked film was 70 oC higher than that of non-cross-linked collagen film, indicating the thermal stability increased when collagen cross-linked with ribose. The cross-linking index was 85.5% for 8 days incubation in cross-linkage. And it was found that the cross-linked film was capable of resisting the degradation by collagenase up to 8 hours; while for non-cross-linked collagen, it is completely degraded within 3 hours. Fu-Yung Huang 黃福永 2010 學位論文 ; thesis 88 zh-TW |
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碩士 === 國立成功大學 === 化學系碩博士班 === 98 === This study was to investigate the extraction methods and the characterization of fish scale collagen from Taiwan Tilapia. The main objective was to focus on the cross-linkage with ribose and to characterize the thermal stability of this cross-linked collagen/ribose film. It was found that the extraction rate is dependent on the concentration of pepsin and extraction time. The optimum condition was as of in pH 2 aqueous solution, extraction time over 24 hours and catalyzed by pepsin with a concentration of mg/mL. The collagen thus extracted was characterized by using Hydroxyproline quantification method, UV and FT-IR spectroscopy, viscometer, differential scanning calorimetry (DSC), Circular Dichroism Spectroscopy (CD), scanning electronic microscope (SEM). The results showed that the concentration of the extracted collagen is 0.937 mg/mL. The band at 230 nm (Histidine) of UV spectrum, the bands at 1661 cm-1, 1546 cm-1, 1239 cm-1of IR spectrum, and the positive band at 223 nm and negative band at 202 nm (triple helix structure) analyzed by CD are the collagen characteristic. The Td of solution in the concentration of (0.3mg/ml) was 33 oC. The Td of lyophilized collagen analyzed by DSC was 73 oC. The optimum cross-linking condition was that the concentration ratio of collagen to ribose is 2mg/ml to 0.2 M and the cross-linking time is 8 hours. The FT-IR spectrum of the cross-linked film showed the coexistence of collogen and ribose.The Td of the cross-linked film was 70 oC higher than that of non-cross-linked collagen film, indicating the thermal stability increased when collagen cross-linked with ribose. The cross-linking index was 85.5% for 8 days incubation in cross-linkage. And it was found that the cross-linked film was capable of resisting the degradation by collagenase up to 8 hours; while for non-cross-linked collagen, it is completely degraded within 3 hours.
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author2 |
Fu-Yung Huang |
author_facet |
Fu-Yung Huang Chien-ChihLin 林建智 |
author |
Chien-ChihLin 林建智 |
spellingShingle |
Chien-ChihLin 林建智 The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
author_sort |
Chien-ChihLin |
title |
The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
title_short |
The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
title_full |
The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
title_fullStr |
The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
title_full_unstemmed |
The study of ribose assisted cross-link of fish scale collagen from Taiwan Tilapia |
title_sort |
study of ribose assisted cross-link of fish scale collagen from taiwan tilapia |
publishDate |
2010 |
url |
http://ndltd.ncl.edu.tw/handle/25182854271636957546 |
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