The influence of hydration and ionizing radiation on denaturation process in keratin

Marzec, E.

doi:10.1016/s0302-4598(98)00137-8

Cited by 4 publications

(2 citation statements)

References 20 publications

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Section: Introductionmentioning

confidence: 99%

“…12,13 When protein is treated by some physical or chemical agents, including high temperature, radiation, acids, and bases, the disulfide and hydrogen bonds are unavoidably broken, which results in the change of secondary structure content. 14,15 This process is generally called protein denaturation. 16 At present, the facile test method for the alteration of keratin secondary structures during treatment and regeneration is not suitable or beneficial for its further application.…”

Section: Introductionmentioning

confidence: 99%

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Second-Order Derivation Fourier Transform Infrared Spectral Analysis of Regenerated Wool Keratin Structural Changes

Jiang

Wang

et al. 2022

AATCC Journal of Research

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Keratin is a natural biopolymer with excellent biocompatibility and biodegradability properties. It is widely used in biomaterial construction. The secondary structure of keratin is essential in its applications. This structure is associated with its regeneration. In this study, the structure of regenerated keratin from wool was analyzed using the amide I, II, and III bands from second-order derivation Fourier transform infrared spectroscopy. The results showed that the regenerated wool keratin retained its molecular backbone with the cleavage of disulfide bonds. The amide I and II bands indicated that the content ratio of α-helix to non-α-helix structure was less in the regenerated keratin than that of raw wool. The amide III band confirmed the contents of α-helix/β-sheet/β-turn/random coil for raw wool (35%/31%/22%/13%) and regenerated keratin (26%/35%/23%/15%).

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