Study on the self-assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods | |
Yan, MY; Qin, S; Li, J; 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 | |
发表期刊 | INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY |
ISSN | 0950-5423 |
2015-09-01 | |
卷号 | 50期号:9页码:2088-2096 |
关键词 | Collagen Extraction Method Fish Skin Self-assembly Tilapia |
DOI | 10.1111/ijfs.12870 |
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 |
作者部门 | 海岸带生物学与生物资源利用所重点实验室 |
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.; 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. |
文章类型 | Article |
收录类别 | SCI |
语种 | 英语 |
关键词[WOS] | PEPSIN-SOLUBILIZED COLLAGEN ; THERAGRA-CHALCOGRAMMA SKIN ; ACID-SOLUBLE COLLAGEN ; PHYSICOCHEMICAL PROPERTIES ; PH ; FIBRILLOGENESIS ; TEMPERATURES ; PROTEINS ; BONE ; FISH |
研究领域[WOS] | Food Science & Technology |
WOS记录号 | WOS:000359859300019 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.yic.ac.cn/handle/133337/10022 |
专题 | 海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室 中国科学院烟台海岸带研究所 |
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 |
推荐引用方式 GB/T 7714 | Yan, MY,Qin, S,Li, J,et al. 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,&Qin, S .(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. |
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