碩士 / 國立高雄海洋科技大學 / 水產食品科學研究所 / 100 / The objective of this study is to establish a process conditions for preparing collagen peptides with iron-binding (Fe-B) activity from seaperch scale, and to isolate, purify and identify the amino acid sequence from the peptides.Four kinds of fish scales were examined and compared for their Fe-B activity, that from Chanos chanos showed the highest activity, followed by Lates calcarifer, Mugil cephalus, and Oreochromis spp. Fish scale from Lates calcarifer was selected and used in the following study. Hydrolysates obtained from fish scales treated with heating and acid showed high Fe-B activity, but lost their activity after artificial digestive juice treatment. Hydrolysates from fish scales treated with papain exhibited the highest Fe-B activity when compared with those treated by other commercial enzymes (alcalase, flavourzyme, protease-N, protamex, bromelain), and its Fe-B activity remained after artificial digestive juice treatment. The optimal conditions in two enzymes system (papain and flavourzyme) were listed as follows: temperature 55℃; pH 8.0; reaction time 2hr; fish scale 8%; 9000U/mL for papain and flavourzyme. The optimal conditions for preparing a collagen peptide powder by spray drying were in inlet/outlet temperature 140℃/80℃. Collagen peptides obtained from two enzymes system were then purified with Hitrap Q HP ion-exchange, Sephadex G-25 gelfiltration and Superdex peptide column chromatography. Two fractions (named Q1 and Q2) with Fe-B activity were obtained from Q HP column separation, Q1 was selected and used in following purification due to its higher Fe-B activity than that of Q2. Three fractions (named Q1G1, Q1G2, Q1G3) were obtained from Sephadex G-25 gelfiltration.Q1G1 and Q1G2 possessing similar Fe-B activity were selected and used in following purification, while Q1G3 showed no Fe-B activity. One fraction (named Q1G1S1) with Fe-B activity obtained from Superdex peptide 10/300 column separation was being identified for its amino acid sequence by LC-MS-MS. According to the infrared spectra of the fish scale collagen peptides and iron-peptides complex, the main iron-binding site was at the carboxylate groups.
| Identifer | oai:union.ndltd.org:TW/100NKIMT084017 |
| Date | January 2012 |
| Creators | Li,Ying-Han, 李英漢 |
| Contributors | Kuo,Jen-Min, 郭建民 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 149 |
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