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Enzymatic phosphorylation of hair keratin enhances fast adsorption of cationic moieties.

International journal of biological macromolecules (2016-01-13)
Vadim Volkov, Artur Cavaco-Paulo
RESUMEN

The current study describes the in vitro phosphorylation of a human hair keratin, using protein kinase for the first time. Phosphorylation of keratin was demonstrated by (31)P NMR (Nuclear Magnetic Resonance) and Diffuse Reflectance Infrared Fourier Transform (DRIFT) techniques. Phosphorylation induced a 2.5 fold increase of adsorption capacity in the first 10 min for cationic moiety like methylene blue (MB). Thorough description of MB adsorption process was performed by several isothermal models. Reconstructed fluorescent microscopy images depict distinct amounts of dye bound to the differently treated hair. The results of this work suggest that the enzymatic phosphorylation of keratins might have significant implications in hair shampooing and conditioning, where short application times of cationic components are of prime importance.

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Sigma-Aldrich
Protease from Bacillus sp., liquid, ≥8 U/g
Sigma-Aldrich
Protein Kinase A from bovine heart, ≥0.8 units/μg protein, lyophilized powder