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
ISSN0950-5423
2015-09-01
卷号50期号:9页码:2088-2096
关键词Collagen Extraction Method Fish Skin Self-assembly Tilapia
DOI10.1111/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
被引频次:18[WOS]   [WOS记录]     [WOS相关记录]
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
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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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