Hen egg white lysozyme as an inhibitor of mushroom tyrosinase

FEBS Letters
Bin LiSusan M Paskewitz

Abstract

We report a kinetics study on hen egg white lysozyme's (HEWL) inhibitory effect on mushroom tyrosinase catalysis of 3-(3,4-dihydroxyphenyl)-L-alanine (L-DOPA) or L-tyrosine. For the first time, we demonstrate HEWL as a robust inhibitor against mushroom tyrosinase in catalysis of both substrates. The kinetics pattern matches a mixed (mostly non-competitive) partial inhibition. Ki and ID50 value of HEWL are more than 20-fold lower than that of kojic acid, a well-known chemical inhibitor of mushroom tyrosinase. Ki, alpha value and beta value, are almost identical in both experiments (L-DOPA and L-tyrosine as substrates, respectively), which suggests this common inhibition mechanism affects both steps. The inhibitory effect increases as both proteins were mixed and pre-incubated for less than 1 h. HEWL-depletion only removed about half of the inhibitory effect. Here we propose a novel function of HEWL, which combines the reversible inhibition and the irreversible inactivation toward mushroom tyrosinase. Discovery of HEWL as an inhibitor to mushroom tyrosinase catalysis may be commercially valuable in the food, medical and cosmetic industries.

References

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Citations

Sep 19, 2009·Applied Biochemistry and Biotechnology·Shu-Bai LiLi-Min Zhu
Jul 8, 2009·International Journal of Molecular Sciences·Te-Sheng Chang
Oct 30, 2009·International Journal of Molecular Sciences·Elizabeth NeeleyWilliam Flurkey
Jan 18, 2013·Journal of Enzyme Inhibition and Medicinal Chemistry·Wei SunKlaus-Heinrich Röhm
Jan 17, 2014·Journal of Biotechnology·Huiqing YuGuoxiang Cheng
Jun 13, 2009·The Journal of Physical Chemistry. B·Karina Kubiak, Paul A Mulheran
Aug 25, 2009·Bioorganic & Medicinal Chemistry Letters·Jin-Mi NohYoon-Sik Lee

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