Abstract：
:Tyrosinase efficiently catalyzes the ortho-hydroxylation of monophenols and the oxidation of diphenols without any additional cofactors. Although it is of significant interest for the biosynthesis of catechol derivatives, the rapid catechol oxidase activity and inactivation of tyrosinase have hampered its practical utilization as a monophenol monooxygenase. Here, we prepared a functional tyrosinase that exhibited a distinguished monophenolase/diphenolase activity ratio (V max mono/ V max di = 3.83) and enhanced catalytic efficiency against L-tyrosine (k cat = 3.33 ± 0.18 s-1, K m = 2.12 ± 0.14 mM at 20 °C and pH 6.0). This enzyme was still highly active in ice water (>80%), and its activity was well conserved below 30 °C. In vitro DOPA modification, with a remarkably high yield as a monophenol monooxygenase, was achieved by the enzyme taking advantage of these biocatalytic properties. These results demonstrate the strong potential for this enzyme's use as a monophenol monooxygenase in biomedical and industrial applications.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Do H,Kang E,Yang B,Cha HJ,Choi YSdoi
10.1038/s41598-017-17635-0subject
Has Abstractpub_date
2017-12-08 00:00:00pages
17267issue
1issn
2045-2322pii
10.1038/s41598-017-17635-0journal_volume
7pub_type
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