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, 3:596

Chemistry and Materials Science


Keratin from the hoof is a less explored source for making valuable products. In this paper we present the extraction of pure keratin from bovine hooves and characterized them to better address the possible exploitation of this bio-resource as an alternative material for tissue engineering applications. The keratin protein from the pulverized hooves was extracted by reduction, which was observed to be pure, and two polypeptide chains of molecular weight in the range of 45–50 and 55–60 KDa were determined using SDS-PAGE assay. FTIR analysis complementing circular dichroism CD data, established that hoof keratin predominantly adopted α-helical conformation with admixture of β-sheet. The keratin was shown to have appreciably high denaturation temperature 215°C as indicated by differential scanning calorimetric DSC analysis. Thermogravimetric analysis TGA also showed the retention of 50% of the original weight of the sample even at a temperature of 346°C. The keratin from the hoof had been observed to be biocompatible when analyzed with MTT assay using fibroblast cells, showing more than 90% cell viability. Hence, hoof keratin would be useful for high value biomedical applications.

KeywordsProteins Keratin Biocompatibility α-helix β-sheet Biopolymers and renewable polymers Electronic supplementary materialThe online version of this article doi:10.1186-2193-1801-3-596 contains supplementary material, which is available to authorized users.

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Autor: Prachi Kakkar - Balaraman Madhan - Ganesh Shanmugam

Fuente: https://link.springer.com/

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