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• W1570494026 endingPage "2096" @default.
• W1570494026 startingPage "2088" @default.
• W1570494026 abstract "Summary Type I collagen was prepared from tilapia ( Oreochromis niloticus ) skin by acetic acid and pepsin process at 4 °C, respectively ( ASC and PSC ), and hot‐water method separately at 25, 35 and 45 °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 °C extraction produced collagen with much reduced proportions of α‐ and β‐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." @default.
• W1570494026 created "2016-06-24" @default.
• W1570494026 creator A5072071608 @default.
• W1570494026 creator A5072494269 @default.
• W1570494026 creator A5084889171 @default.
• W1570494026 date "2015-07-27" @default.
• W1570494026 modified "2023-10-04" @default.
• W1570494026 title "Study on the self-assembly property of type I collagen prepared from tilapia (<i>Oreochromis niloticus</i>) skin by different extraction methods" @default.
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• W1570494026 doi "https://doi.org/10.1111/ijfs.12870" @default.
• W1570494026 hasPublicationYear "2015" @default.
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