Characteristics of collagen from the skin of clown featherback (Chitala ornata)

Abstract

Extraction Clown featherback skinFreeze-drying -82.08% total collagen recovery -27.64% yield of ASC -44.63% yield of PSC -330-333 residues/1000 residues of glycine -201-202 residues/1000 residues of imino acid -type I, comprising (α1) 2 α2-heterotrimer -T max = 35.23-36.28 °C -pI = 5.54-5.68 Salt precipitation Dialysis Characteristics of collagen Collagen ExtractionGraphical Abstract and PSC were 27.64 and 44.63% (dry weight basis) with total collagen recovery of 29 82.08%. Both collagens contained glycine as the major amino acid with relatively 30 high content of proline, hydroxyproline and glutamic acid/glutamine. Nevertheless, 31 they had the low content of cysteine, histidine and tryrosine. The collagen was 32 characterised as type I, comprising (α1) 2 α2-heterotrimer. Pepsin-aided process did not 33 affect triple-helical structure of PSC as determined by FTIR spectra. Thermal 34 transition temperature of ASC (36.28 °C) was slightly higher than that of PSC (35.23 35 °C). However, no differences in isoelectirc point (5.54-5.68) between ASC and PSC 36 was observed. Therefore, collagen from the skin of clown featherback could be 37 successfully extracted for further applications. 38 39

Characterization and Antioxidant Activity of Collagen, Gelatin, and the Derived Peptides from Yellowfin Tuna (Thunnus albacares) Skin

“…It is known that optimal pH value can make it easier to apply the material to the product. Neutral pH facilitates the interaction of proteins with water molecules, thereby improving the solubility [28].…”

Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process

“…In fresh muscle, various protein fractions were separated within the tested pH range (4 to 7), and these fractions presented different profiles compared to the isoelectric point reported for collagen extracted with acidic solutions (pH 6 to 7). [30] These differences could be attributed to the presence of different collagen types depending on the anatomical region from which the extraction was carried out. Since the electrophoretic profile observed in the SDS-PAGE also revealed differences between the protein bands detected in each analyzed fraction ( Fig.…”

“…[18] In different squid species, a type I collagen has been reported, with higher proportion of β chain (cross-linked component) compared to α chains. [20,23,30] Type I collagen is the most common collagen, and is formed by three polypeptide chains: two of the strands (denominated α1) have an identical amino-acid sequence, whereas the third one (denominated α2) has a different amino-acid sequence. [31] Another type of collagen found in the muscle is Type III.…”

Optimization of Time and Temperature Gelatin Extraction from Pink Perch (Nemipterus bathybius) Head using Response Surface Methodology (RSM)

“…However, the issue of BSE (Bovine Spongiform Encephalopathy) disease and differences in consumer belief is a problem for consuming bovine or porcine gelatin. Therefore, gelatin obtained from the industrial waste of fish processing can be used as an alternative source of gelatin [3].…”