Extraction and Characterization of Acid-Soluble and Pepsin-Soluble Collagen from Giant Salamander Bone

被引：0
|
作者：
Gong X. [1 ]
Bao J. [1 ]
Huang K. [1 ]
Chen Y. [1 ]
Tang J. [1 ]
机构：
[1] College of Food Science, Shanghai Ocean University, Shanghai
来源：
Journal of Chinese Institute of Food Science and Technology | 2024年 / 24卷 / 03期
关键词：
characterization; collagen; extraction; giant salamander bone;
D O I：
10.16429/j.1009-7848.2024.03.027
中图分类号：
学科分类号：
摘要：
The giant salamander, as a precious amphibian, is rich in nutritional value. To fully and efficiently utilize its processing by-products, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from giant salamander bone were isolated and characterized. The yields of salamander bone ASC and PSC were 10.71% and 13.11%, respectively. The stable triple helical structure of collagen was revealed by Fourier transform infrared spectroscopy. SDS-PAGE electropherograms showed that both samples were type I collagen with high levels of imino acids (179-187/1 000 residues). Their solubility was highest at pH 6. The thermal denaturation temperature (45.78-46.51 ℃) was significantly higher than that of marine and freshwater fish species. Under SEM, the collagen showed dense flakes and irregular holes. These results show that the characteristics of giant salamander bone collagen are similar to mammalian collagen, and it has the potential to become its substitute, which provides a basis for its subsequent research and development and utilization. © 2024 Chinese Institute of Food Science and Technology. All rights reserved.
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页码：268 / 275
页数：7
相关论文
共 31 条
  • [1] YAN F, LU J, ZHANG B Z, Et al., The Chinese giant salamander exemplifies the hidden extinction of cryptic species, Current Biology, 28, 10, pp. 590-592, (2018)
  • [2] GENG X F, WEI H, SHANG H T, Et al., Proteomic analysis of the skin of Chinese giant salamander (Andrias davidianus), Journal of Proteomics, 2, (2015)
  • [3] HADFI N H, SARBON N M., Physicochemical properties of silver catfish (Pangasius sp.) skin collagen as influenced by acetic acid concentration, Food Research, 3, 6, pp. 783-790, (2019)
  • [4] YU H., Preparation and antioxidant of collagen from deer bone, (2016)
  • [5] URIARTE-MONTOYA M H, ARIAS-MOSCOSO J L, PLASCENCIA-JATOMEA M, Et al., Jumbo squid (Dosidicus gigas) mantle collagen: extraction, characterization, and potential application in the preparation of chitosan-collagen biofilms, Bioresource Technology, 101, 11, pp. 4212-4219, (2010)
  • [6] AHMED R, HAQ M, CHUN B S., Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus), International Journal of Biological Macromolecules, 135, pp. 668-676, (2019)
  • [7] LAEMMLI U K, QUITTNER S F., Maturation of the head of bacteriophage T4. IV. The proteins of the core of the tubular polyheads and in vitro cleavage of the head proteins, Virology, 62, 2, pp. 483-499, (1974)
  • [8] LIU W, LI G, MIAO Y, Et al., Preparation and characterization of pepsin-solubilized type I collagen from the scales of snakehead (Ophiocephalus argus), Journal of Food Biochemistry, 33, 1, pp. 20-37, (2009)
  • [9] REGENSTEIN J M, ZHOU P., Collagen and gelatin from marine by-products, Maximising the Value of Marine By-Products, pp. 279-303, (2007)
  • [10] DUAN R, ZHANG J J, DU X Q, Et al., Properties of collagen from skin, scale and bone of carp (Cyprinus carpio), Food Chemistry, 112, 3, pp. 702-706, (2008)
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