Abstract
Nowadays, biopolymers such as keratins are widely used in biomedicine due to their low toxicity, biocompatibility, and biodegradability. At the molecular level, keratins differ from other structural proteins by a high content of disulfide bonds, which provide the formation of a compact three-dimensional structure resistant to biological and chemical degradation. Native keratins are highly ordered, whereas, recovered keratins are characterized by a flexible structure with more accessible functional groups. A characteristic feature of solubilized keratins is their ability to polymerize; therefore, they are widely used to create biomaterials. The extraction of keratins from natural fibers is an important step to the development of functional biomaterials. However, this process is complicated by the presence of a large number of intramolecular and intermolecular disulfide bonds in keratins. That is why keratin extraction by breaking the intermolecular disulfide bonds while preserving the covalent bonds of the polypeptide chain is necessary. The goal of our study was to estimate the different methods of solubilized keratin obtaining. In the experiments, samples of different types of wool and human hair were used. Various methods of keratin extraction were applied. The yield of solubilized keratin (%) was calculated from the ratio of the weight of the lyophilized keratin extract and the initial weight of fibers. The molecular mass of recovered keratins was evaluated by SDS-PAAG electrophoresis in the Laemmli buffer system. An analysis of the efficiency of keratin extraction has shown that solubilized keratin yield ranged from 32% to 51% and depended on the composition of the extraction mixture. Electrophoretic analysis of all keratin extracts obtained by various methods confirmed the presence of two bands, which according to the molecular weight corresponding to I and II types of proteins of intermediate filaments. The presence of these proteins provides self-assembly into complex structures.
Highlights
On the other hand, keratin is a biopolymer with a strongly hierarchical organization of subunits, from the α-chains, via intermediate filaments, to the fiber
Keratins differ from other structural proteins by a high content of disulfide bonds, which provide the formation of a compact three-dimensional structure resistant to biological and chemical degradation
Keratins differ from other structural proteins by a high content of cysteine, and disulfide bonds, which provide the formation of a compact three-dimensional structure resistant to biological and chemical degradation
Summary
Keratin is a biopolymer with a strongly hierarchical organization of subunits, from the α-chains, via intermediate filaments, to the fiber. It is known that extracted keratin is characterized by the ability to self-assembly and self-aggregation [17]. The extraction of keratins from human hair and animal fibers is the first step towards the development of biomaterials with a high degree of functionality. It is important to save the natural characteristics of recovered keratin breaking only intermolecular disulfide bonds and preserving the covalent bonds of the polypeptide chain. The obtained recovered keratin and its physicochemical characteristics significantly depend on the source and method of extraction. In this regard, the purpose of our study was to obtain soluble keratin from wool and human hair and evaluate the efficacy of keratin recovery
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