Structural feature and self-assembly properties of type II collagens from the cartilages of skate and sturgeon.
Amino Acids
/ analysis
Animals
Cartilage
/ chemistry
Circular Dichroism
Collagen Type II
/ analysis
Fish Products
Fish Proteins
/ analysis
Fishes
Hydrogen-Ion Concentration
Monosaccharides
/ analysis
Osmolar Concentration
Pepsin A
/ chemistry
Protein Conformation
Skates, Fish
Sodium Chloride
/ chemistry
Solubility
Spectroscopy, Fourier Transform Infrared
X-Ray Diffraction
Cartilage
Self-assembly properties
Skate
Structural feature
Sturgeon
Type II collagen
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 Nov 2020
30 Nov 2020
Historique:
received:
05
12
2019
revised:
25
05
2020
accepted:
12
06
2020
pubmed:
23
6
2020
medline:
21
10
2020
entrez:
23
6
2020
Statut:
ppublish
Résumé
Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and purified from the cartilages of skate and sturgeon. Their typical structure and physicochemical properties were evaluated by circular dichroism (CD), X-ray diffraction (XRD), and so on. Results showed that the extracted collagen was likely identified as collagen-II composed of three α-chains (135 kDa), with the typical peptide sequence of Gly-X-Y. It showed the collagen retained the native and intact triple helical structure, and its intensity ratio of the positive and negative absorption peaks (Rpn) was 0.19-0.25. In addition, the extracted collagen exhibited obvious self-assembly behavior with the concentration above 0.3 mg/mL, the adjustment of pH 7.4-7.6 and the NaCl concentration of 120 mmol/L. The critical aggregate mass concentrations of pepsin-soluble collagens from skate and sturgeon were 0.93 and 0.86 g/L, respectively. Therefore, collagens from skate and sturgeon cartilages have potential commercial application.
Identifiants
pubmed: 32569971
pii: S0308-8146(20)31202-4
doi: 10.1016/j.foodchem.2020.127340
pii:
doi:
Substances chimiques
Amino Acids
0
Collagen Type II
0
Fish Proteins
0
Monosaccharides
0
Sodium Chloride
451W47IQ8X
Pepsin A
EC 3.4.23.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
127340Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.