OBTAINING COLLAGEN HYDROLYSATE FROM CATTLE HIDE WASTE
Authors
Jumayev Nosirbek Abdullayevich, Muydinov Nurillo To‘xtarovich, Radjabov Otabek Iskandarovich, Turayev Abbaskhan Sabirkhanovich
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Hide processing wastes are collagen-rich biomass from which value-added protein hydrolysates can be obtained. In this work, cattle hide waste was treated with 3% NaOH at 20–25 °C for 80 h, washed, heated at 70 °C for 3 h, settled, and neutralized from pH 13.2 to pH 6.75. The alkali-treated hide formed a slurry-like mass and dissolved rapidly upon heating. The product was characterized by Fourier-transform infrared (FTIR) spectroscopy, UV–Vis spectrophotometry (200–800 nm), and reduced viscosity (ηred = 0.083 dL/g). In the FTIR spectrum, amide A, I, II, and III bands were observed at approximately 3273, 1638, 1545, and 1239 cm−1, respectively, confirming that the peptide backbone was preserved. The amide I band was located at a lower wavenumber than the ≈1650 cm−1 characteristic of native collagen, and the amide III/1450 cm−1 absorbance ratio was 0.67; both indicate a significant loss of the triple-helical order. The UV–Vis spectrum showed a maximum at 218 nm (A = 2.931, near the linear limit of the instrument), weak absorption at 280 nm (A = 0.049), and negligible absorbance in the 400–800 nm range. The three methods together demonstrate that the treatment yields a neutral, optically clear, partially hydrolyzed, and conformationally disordered collagen derivative.
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Authors
Jumayev Nosirbek Abdullayevich, Muydinov Nurillo To‘xtarovich, Radjabov Otabek Iskandarovich, Turayev Abbaskhan Sabirkhanovich
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References:
Gelse, K.; Pöschl, E.; Aigner, T. Collagens—structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 2003, 55, 1531–1546. https://doi.org/10.1016/S0169-409X(03)00133-9
Gómez-Guillén, M.C.; Giménez, B.; López-Caballero, M.E.; Montero, M.P. Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocoll. 2011, 25, 1813–1827. https://doi.org/10.1016/j.foodhyd.2011.02.007
Banerjee, P.; Madhu, S.; Chandra Babu, N.K.; Shanthi, C. Bio-mimetic mineralization potential of collagen hydrolysate obtained from chromium tanned leather waste. Mater. Sci. Eng. C 2015, 49, 338–347. https://doi.org/10.1016/j.msec.2015.01.027
Brooker, C.; Tronci, G. Effect of mammalian tissue source on the molecular and macroscopic characteristics of UV-cured type I collagen hydrogel networks. Prosthesis 2022, 4, 1–14. https://doi.org/10.3390/prosthesis4010001
Kristoffersen, K.A.; Måge, I.; Wubshet, S.G.; Böcker, U.; Dankel, K.R.; Lislelid, A.; Rønningen, M.A.; Afseth, N.K. FTIR-based prediction of collagen content in hydrolyzed protein samples. Spectrochim. Acta A 2023, 301, 122919. https://doi.org/10.1016/j.saa.2023.122919
Chen, X.; Meng, J.; Xu, H.; Shinoda, M.; Kishimoto, M.; Sakurai, S.; Yamane, H. Fabrication and properties of electrospun collagen tubular scaffold crosslinked by physical and chemical treatments. Polymers 2021, 13, 755. https://doi.org/10.3390/polym13050755
Wang, S.-S.; Yu, Y.; Sun, Y.; Liu, N.; Zhou, D.-Q. Comparison of physicochemical characteristics and fibril formation ability of collagens extracted from the skin of farmed river puffer (Takifugu obscurus) and tiger puffer (Takifugu rubripes). Mar. Drugs 2019, 17, 462. https://doi.org/10.3390/md17080462
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