Study on the self-assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods
文献类型：期刊论文
| 作者 | Yan, MY ; Qin, S; Li, J
|
| 刊名 | INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
 |
| 出版日期 | 2015-09-01 |
| 卷号 | 50期号:9页码:2088-2096 |
| 关键词 | Collagen extraction method fish skin self-assembly tilapia |
| ISSN号 | 0950-5423 |
| 产权排序 | [Yan, Mingyan] Qingdao Univ Sci & Technol, Coll Chem & Mol Engn, Qingdao 266042, Peoples R China; [Qin, Song; Li, Jie] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Shandong, Peoples R China |
| 通讯作者 | Qin, S (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res, 17 Chunhui Rd, Yantai 264003, Shandong, Peoples R China. myyan@yic.ac.cn |
| 中文摘要 | Type I collagen was prepared from tilapia (Oreochromis niloticus) skin by acetic acid and pepsin process at 4 degrees C, respectively (ASC and PSC), and hot-water method separately at 25, 35 and 45 degrees C (C-25, C-35 and C-45). Their structure and self-assembly property were discussed. SDS-PAGE patterns suggested that pepsin hydrolysis and the 35 and 45 degrees C extraction produced collagen with much reduced proportions of - and -chains. Fourier transform infrared spectroscopy spectra revealed that pepsin hydrolysis did not change the conformation of collagen, but higher extraction temperature did. Self-assembly curves and atomic force microscopy (AFM) observations showed that only ASC, PSC and C-25 could self-assemble into fibrils with D-periodicity, but the reconstruction rate of C-25 was lower. Besides, PSC had relatively higher resolution ratio compared with others. Overall, pepsin-extracted collagen displayed higher solubility and better fibril-forming capacity, having the potential of applying in biomaterials and food-packaging materials. |
| 英文摘要 | Type I collagen was prepared from tilapia (Oreochromis niloticus) skin by acetic acid and pepsin process at 4 degrees C, respectively (ASC and PSC), and hot-water method separately at 25, 35 and 45 degrees C (C-25, C-35 and C-45). Their structure and self-assembly property were discussed. SDS-PAGE patterns suggested that pepsin hydrolysis and the 35 and 45 degrees C extraction produced collagen with much reduced proportions of - and -chains. Fourier transform infrared spectroscopy spectra revealed that pepsin hydrolysis did not change the conformation of collagen, but higher extraction temperature did. Self-assembly curves and atomic force microscopy (AFM) observations showed that only ASC, PSC and C-25 could self-assemble into fibrils with D-periodicity, but the reconstruction rate of C-25 was lower. Besides, PSC had relatively higher resolution ratio compared with others. Overall, pepsin-extracted collagen displayed higher solubility and better fibril-forming capacity, having the potential of applying in biomaterials and food-packaging materials. |
| 研究领域[WOS] | Food Science & Technology |
| 关键词[WOS] | PEPSIN-SOLUBILIZED COLLAGEN ; THERAGRA-CHALCOGRAMMA SKIN ; ACID-SOLUBLE COLLAGEN ; PHYSICOCHEMICAL PROPERTIES ; PH ; FIBRILLOGENESIS ; TEMPERATURES ; PROTEINS ; BONE ; FISH |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000359859300019 |
| 源URL | [http://ir.yic.ac.cn/handle/133337/10022]  |
| 专题 | 烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室 中国科学院烟台海岸带研究所 |
| 推荐引用方式 GB/T 7714 | Yan, MY,Qin, S,Li, J. Study on the self-assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods[J]. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY,2015,50(9):2088-2096. |
| APA | Yan, MY,Qin, S,&Li, J.(2015).Study on the self-assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods.INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY,50(9),2088-2096. |
| MLA | Yan, MY,et al."Study on the self-assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods".INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY 50.9(2015):2088-2096. |
入库方式： OAI收割
来源：烟台海岸带研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。