Characterization of Acid-soluble Collagen from the Skin of Hammerhead Shark (Sphyrna lewini )

Abstract

The characteristics of the acid-soluble collagen (ASC) from the skin of hammerhead shark (Sphyrna lewini) (ASC-H) were investigated and compared with those of calf skin collagen (CSC). ASC-H with a yield of 4.23 ± 0.54% (based on the wet weight of skins) contained Gly (227 residues/1,000 residues) as the major amino acid and had imino acids of 205 residues/1,000 residues. Amino acid composition, sodium dodecyl sulfate polyacrylamide gel electrophoresis pattern and Fourier transform spectroscopy (FTIR), confirmed that ASC-H was mainly composed of type I collagen. The peptide map of ASC-H was different from that of CSC, suggesting the differences in amino acid sequences and conformation. Td of ASC-H was 16.89C, which was similar to those of cold-water fishes but significantly lower than those of tropical fish species and mammals. ASC-H exhibited high solubility in pH (1-4) and low NaCl concentrations (≤3%). In addition, the lyophilized collagen displayed loose, fibrous and porous ultrastructure. PRACTICAL APPLICATIONSAt present, large quantities of by-products, accounting for 50-70% of the original raw material, are generated during the process of aquatic products processing industry. Therefore, optimal use of these by-products is a promising way to protect the environment and produce value-added products to increase the revenue of fish processors. Recently, many scientists have focused their interests on isolation and characterization of collagens extracted from skins of aquatic organisms. However, no information regarding acid-soluble collagen (ASC) from skins of Hammerhead shark (Sphyrna lewini) has been reported. The aim of this study was to isolate and characterize ASC from skin of Hammerhead shark in comparison with type I collagen from calf skin (CSC). Therefore, the collagen extracted from the skin of hammerhead shark could bring considerably economic benefits as a substitute for mammalian collagen.

Physicochemical and Antioxidant Properties of Acid- and Pepsin-Soluble Collagens from the Scales of Miiuy Croaker (Miichthys Miiuy)

“…Amide I, amide II and amide III bands are bound up with the triple helical structure of collagen, resulting from C=O stretching, N–H bending and C–H stretching, respectively [ 9 , 26 ]. The amide I band with strong absorbance in the range of 1600–1700 cm −1 is primarily associated with the C=O stretching vibration along the polypeptide backbone or a hydrogen bond coupled with COO– and the decrease of molecular order will make the peak shift to lower wavenumber [ 19 ].…”

“…Therefore, the enormous demand for collagen from alternative resources such as aquatic byproducts (skin, bone, swim bladder, scale and fins) has increased for many years due to no dietary restriction and risk of disease transmission [ 3 , 8 ]. Furthermore, effective use of aquatic byproducts to produce high value-added products is an important way to increase the income to the fish processor and protect the environment [ 9 ].…”

Anti-Fatigue Effect by Peptide Fraction from Protein Hydrolysate of Croceine Croaker (Pseudosciaena crocea) Swim Bladder through Inhibiting the Oxidative Reactions including DNA Damage

“…The amino acid composition of SBP-III-3 was analyzed according to the previous method [46]. To determine the amino acid composition, freeze-dried SBP-III-3 was dissolved in distilled water to obtain a concentration of 1 mg/mL, and an aliquot of 50 mL was dried and hydrolyzed in a vacuum-sealed glass tube at 110 °C for 24 h in the presence of 6 M HCl, which contained 0.1% phenol.…”

Extraction and characterization of acid-soluble collagen and pepsin-soluble collagen from the dry scales of the striped snakehead (Channa striatus)

“…Hasil penelitian ini sesuai dengan hasil penelitian Matmaroh et al (2011), Di et al (2014), dan Chuaychan et al (2015) yang melaporkan bahwa glisina merupakan asam amino yang dominan pada kolagen dan semua famili kolagen dicirikan oleh adanya pengulangan dari sekuen asam amino Gly-X-Y, X adalah prolina dan Y hidroksiprolina. Asam imino berupa prolina dan hidroksiprolina penting untuk integritas struktural kolagen, karena berperan penting dalam pembentukan ikatan hidrogen intramolekul (Chi et al 2014). Jumlah asam imino KLA-SH dan KLP-SH masing-masing yaitu 226 dan 230 residu/1.000 residu.…”