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Effects of superfine silk protein powders on mechanical properties of wet-spun polyurethane fibers

Authors

  • Hongtao Liu,

    1. College of Textiles, Donghua University, Shanghai 201620, People's Republic of China
    2. Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
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  • Weilin Xu,

    Corresponding author
    1. Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
    • Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
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  • Xiuying Liu,

    1. Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
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  • Jie Xu,

    1. Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
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  • Wenbin Li,

    1. Key Laboratory for Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Wuhan 430073, People's Republic of China
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  • Xin Liu

    1. College of Textiles, Donghua University, Shanghai 201620, People's Republic of China
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Abstract

Mechanical measurements were employed to investigate the effects of three types of superfine silk protein powder on tensile strength, elongation, and elasticity of wet-spun Pellethane® 2363-80AE polyurethane (PU) fiber. These superfine silk protein powders included undegummed silk (with both native silk fibroin and sericin, water insoluble), native silk fibroin (with native silk fibroin only, water insoluble), and regenerated silk fibroin (with regenerated silk fibroin only, water soluble) in powder form. Experimental data derived from the mechanical measurements illustrated that the miscibility between the PU and regenerated silk fibroin were superior to that between PU and the other two silk proteins. This may be attributed to the similar chemical structure and microphase separation of PU and regenerated silk fibroin with lower molecular weight than native silk fibroin. This preliminary work may provide some information for biomimetic processing of silk-inspired PU biofibers, which combine elasticity of synthetic PU with biofunction of natural silk fibroin for special biomedical applications. © 2009 Wiley Periodicals, Inc. J Appl Polym Sci, 2009

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