Physicochemical properties of acid- and pepsin-soluble collagens from the cartilage of Siberian sturgeon
- 100 Downloads
To look for the collagen alternatives of mammalian cartilages from aquatics and their by-products, acid-soluble collagen (ASC-SC) and pepsin-soluble collagen (PSC-SC) were extracted from cartilages of Siberian sturgeon (Acipenser baerii) with yields of 27.13 ± 1.15 and 14.69 ± 0.85% on dry weight basis. ASC-SC and PSC-SC had glycine as the major amino acid with the contents of 326.8 and 327.5 residues 1000 residues−1, and their contents of proline and hydroxyproline were 205.9 and 208.0 residues 1000 residues−1. ASC-SC and PSC-SC comprised type I collagen ([α1(I)]2α2(I)) and type II collagen ([α1(II)]3) on the literatures and results of amino acid composition, SDS-PAGE pattern, UV, and FTIR spectra. Meanwhile, FTIR spectra data indicated that there were more hydrogen bonds in ASC-SC and more intermolecular crosslinks in PSC-SC. The maximum transition temperature (Tmax) of the ASC (28.3 °C) and PSC (30.5 °C) was lower than those of collagens from mammalian cartilages (> 37 °C). ASC-SC and PSC-SC showed high solubility in the acidic pH ranges and the solubility decreased in the presence of NaCl at concentrations above 3%. Zeta potential studies indicated that both ASC-SC and PSC-SC exhibited a net zero charge at pH 6.30 and 6.32. SEM results indicated that ASC-SC and PSC-SC presented irregular dense sheet-like film linked by random-coiled filaments. Therefore, collagens from Siberian sturgeon cartilages might be the suitable alternatives of the collagens of mammal cartilages as functional ingredient to treat some diseases.
KeywordsSiberian sturgeon (Acipenser baerii) Cartilage Acid-soluble collagen (ASC) Pepsin-soluble collagen (PSC) Antioxidant activity
This work was funded by the National Natural Science Foundation of China (NSFC) (No. 81673349), Science and Technology Program of Zhoushan (No. 2016C41016), Natural Science Foundation of Zhejiang Province, China (No. LY15C190010), and Open Foundation from Marine Sciences in the Most Important Subjects of Zhejiang (No. 20160116).
Compliance with ethical standards
Conflicts of interest
The authors declare that they have no conflicts of interest.
- AOAC (2003) Official methods of analysis of AOAC international (17th ed.). Association of the Official Analytical Chemists (AOAC) International, GaithersburgGoogle Scholar
- Asghar A, Henrickson RL (1982) Chemical, biochemical, functional and nutritional characteristics of collagen in food systems. In: Chichester CO, Marata EM, Schweigert BS (eds) Advances in food research. Academic, London, pp 237–273Google Scholar
- Foegeding EA, Laneir TC, Hultin HO (1996) Characteristics of edible muscle tissues. In: Fennema OR (ed) Food chemistry. Marcel Dekker Inc., New York, pp 902–906Google Scholar
- Krishnamoorthi J, Ramasamy P, Shanmugam V, Shanmugam A (2017) Isolation and partial characterization of collagen from outer skin of Sepia pharaonis (Ehrenberg, 1831) from Puducherry coast. Biochem Biophys Rep 10:39–45Google Scholar
- Piez KA, Gross J (1960) The amino acid composition of some fish collagens: the relation between composition and structure. J Biol Chem 235(4):995–998Google Scholar
- Wong DWS (1989) Mechanism and theory in food chemistry. Van Nostrand Reinhold Company Inc., New YorkGoogle Scholar
- Yu D, Chi CF, Wang B, Ding GF, Li Z (2014) Characterization of acid and pepsin soluble collagens from spine and skull of skipjack tuna (Katsuwonus pelamis). Chin J Nat Med 12(9):712–720Google Scholar