Polymerization of Horseradish Peroxidase by a Laccase-Catalyzed Tyrosine Coupling Reaction

Biotechnology Journal
Dani PermanaNoriho Kamiya

Abstract

The polymerization of proteins can create newly active and large bio-macromolecular assemblies that exhibit unique functionalities depending on the properties of the building block proteins and the protein units in polymers. Herein, the first enzymatic polymerization of horseradish peroxidase (HRP) is reported. Recombinant HRPs fused with a tyrosine-tag (Y-tag) through a flexible linker at the N- and/or C-termini are expressed in silkworm, Bombyx mori. Trametes sp. laccase (TL) is used to activate the tyrosine of Y-tagged HRPs with molecular O2 to form a tyrosyl-free radical, which initiates the tyrosine coupling reaction between the HRP units. A covalent dityrosine linkage is also formed through a HRP-catalyzed self-crosslinking reaction in the presence of H2 O2 . The addition of H2 O2 in the self-polymerization of Y-tagged HRPs results in lower activity of the HRP polymers, whereas TL provides site-selectivity, mild reaction conditions and maintains the activity of the polymeric products. The cocrosslinking of Y-tagged HRPs and HRP-protein G (Y-HRP-pG) units catalyzed by TL shows a higher signal in enzyme-linked immunosorbent assay (ELISA) than the genetically pG-fused HRP, Y-HRP-pG, and its polymers. This new enzymatic polym...Continue Reading

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Citations

Jun 18, 2019·Biotechnology Journal·Sung Ok HanYong-Su Jin
Jan 19, 2021·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Dani PermanaNoriho Kamiya
Apr 10, 2021·APL Bioengineering·Wonmoon SongNathaniel S Hwang
Jan 28, 2022·Biotechnology Letters·Dani PermanaDjaenudin Djaenudin

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