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Green Synthesis and Characterization of Hybrid Collagen–Cellulose–Albumin Biofibers from Skin Waste

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Abstract

Collagen (C) and cellulose are prominent biopolymers from the animal and plant kingdom and widely used in bioengineering. Albumin, on the other hand, is the most abundant plasma protein present in mammalian blood. In this work, collagen extracted from animal skin waste was blended with hydroxyethyl cellulose (HEC) and bovine serum albumin (A) and wet-spun to form hybrid biodegradable C/HEC/A fibers. They were further cross-linked with glutaraldehyde vapors and analyzed. X-ray diffraction and infra-red spectroscopic studies of the hybrid fibers display peaks corresponding to collagen, cellulose, and albumin. Incorporation of cellulose into the biopolymeric matrix leads to a reasonable improvement in mechanical, swelling, and thermal properties of hybrid fibers. Addition of albumin improves the regularity of fiber surface without altering the porosity as observed under a microscope. Hence, the formed hybrid biofibers can be potentially used as a suture material as well as for different biomedical applications due to their improved properties.

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Acknowledgments

The authors thank CSIR for providing financial support under CSIR-Young Scientist Award (YSA) and ZERIS project schemes.

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Authors and Affiliations

  1. Advanced Materials Laboratory, Center for Leather Apparel and Accessories Development, Central Leather Research Institute (Council of Scientific and Industrial Research), Adyar, Chennai, 600 020, India

    Manickam Amsaveni, Ayyappan Anumary, Meiyazhagan Ashokkumar, Bangaru Chandrasekaran & Palanisamy Thanikaivelan

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  1. Manickam Amsaveni
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  2. Ayyappan Anumary
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  3. Meiyazhagan Ashokkumar
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  4. Bangaru Chandrasekaran
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  5. Palanisamy Thanikaivelan
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Correspondence to Palanisamy Thanikaivelan.

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Amsaveni, M., Anumary, A., Ashokkumar, M. et al. Green Synthesis and Characterization of Hybrid Collagen–Cellulose–Albumin Biofibers from Skin Waste. Appl Biochem Biotechnol 171, 1500–1512 (2013). https://doi.org/10.1007/s12010-013-0445-2

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  • DOI: https://doi.org/10.1007/s12010-013-0445-2

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