Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods |
| |
Authors: | Mingyan Yan Song Qin Jie Li |
| |
Affiliation: | 1. College of Chemistry and Molecular Engineering, Qingdao University of Science and Technology, China;2. Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, Shandong Province, China |
| |
Abstract: | 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. |
| |
Keywords: | Collagen extraction method fish skin self‐assembly tilapia |
|
|