Characterization of Collagen from Sakhalin Taimen Skin as Useful Biomass

Abstract

Research background. Animal collagen has been widely utilized in foods, cosmetics, and biomedical fields. The non-edible portion, such as fish skins and bones, are generated during cooking processes. Most of them are currently discarded as wastes, although the nutritional values of the skins and bones are high. It needs to utilize the non-edible portion for the reduction of environmental impact, as it may be one of source of environmental pollution. Experimental approach. Collagen was prepared from Sakhalin taimen skins as wastes generated during cooking processes. Next, the color, SDS-polyacrylamide gel electrophoresis, ultraviolet absorption, subunit composition, amino acid composition, denaturation temperature, and attenuated total reflectance-Fourier transform infrared spectroscopy analysis were conducted to explore the properties of the collagen. Lastly, it tried to improve the functional properties of the collagen using chemical modification technique for future applications. Results and conclusions. Cold acetone treatment made it possible to easily remove the fats and pigments from skins. The odorless and pure-white collagen was obtained with high-yield. The α3 chain did not exist in the collagen. Sakhalin taimen skin collagen had rich α-helix and low β-sheet structures. Succinylation caused the secondary structural changes of the collagen molecule. Moreover, succinylation made it possible not only to increase the viscosity of collagen solution and but also to improve the solubility of collagen in the physiological conditions around pH=6. Novelty and scientific contribution. This finding was the first report on the absence of the α3 chain in Salmonid fish skin collagens. The succinylated collagen from Sakhalin taimen skins as useful biomass has potential to utilize in foods, cosmetics, and its related industries.

Sustainable Collagen Blends with Different Ionic Liquids for Resistive Touch Sensing Applications

“…The interactions among the different components of the films and the effect of the ILs on the integrity of collagen structure were assessed by analysis of the FTIR spectra presented in Figure . All of the spectra show the characteristic absorption bands assigned to the peptide bonds in collagen (Figure a): 3500–3000 cm –1 for amide A (N–H stretching), 1632 cm –1 for amide­(I) (CO stretching), 1547 cm –1 for amide­(II) (N–H bending), and 1238 cm –1 for amide­(III) (C–N stretching). , Furthermore, the amide A band, corresponding to the N–H stretching vibration, appears at 3300 cm –1 , instead of 3400 cm –1 , indicating that the NH group is involved in hydrogen bonding. , The spectral region between 1200 and 900 cm –1 is attributed to the stretching vibrations of C–O bonds in collagen and those related to the hydroxyl groups in glycerol. The band at 1043 cm –1 is assigned to the stretching of C–O linkages in C1 and C3 of glycerol, and the band at 1110 cm –1 is related to the stretching of C–O in C2 of glycerol …”

“… 39 , 40 Furthermore, the amide A band, corresponding to the N–H stretching vibration, appears at 3300 cm –1 , instead of 3400 cm –1 , indicating that the NH group is involved in hydrogen bonding. 41 , 42 The spectral region between 1200 and 900 cm –1 is attributed to the stretching vibrations of C–O bonds in collagen and those related to the hydroxyl groups in glycerol. The band at 1043 cm –1 is assigned to the stretching of C–O linkages in C1 and C3 of glycerol, and the band at 1110 cm –1 is related to the stretching of C–O in C2 of glycerol.…”

Emerging Roles of Post-Translational Modifications in Skin Diseases: Current Knowledge, Challenges and Future Perspectives

“…Although many of them have been discovered for many years, only in the last decade the crucial roles of PTMs have attracted considerable attention of researchers in dermatology due to discoveries concerning their enzymology, function and mechanism. Moreover, with the advent of new proteomic techniques, new types of PTMs have shown their importance in various skin diseases, such as carbamylation, 62 succinylation, 63 etc. Accumulating scientific and clinical evidences support that these PTMs regulate diverse cellular process such as cell differentiation, proliferation, inflammation, metastasis and autophagy.…”