Abstract
Objectives
To obtain an acidic and cold-active tyrosinase, which potentially minimizes unwanted self-oxidation of tyrosinase-catalyzed catechols, including 3,4-dihydroxyphenylalanine at elevated pH and high temperature.
Results
A putative psychrophilic tyrosinase (named as tyrosinase-CNK) was identified from the genome information of the marine archaeon Candidatus Nitrosopumilus koreensis. This protein contains key tyrosinase domains, such as copper-binding domains and an O2-binding motif, and phylogenetic analysis revealed that it was distinct from other known bacterial tyrosinases. Functional tyrosinase-CNK was produced by applying a co-expression strategy together with chaperone proteins in Escherichia coli with a yield of approx. 30 mg l−1 and a purity >95 %. The purified enzyme showed optimal activity at pH 6 and 20 °C and still had 50 % activity at 0 °C. Surprisingly, the enzyme exhibited an abnormally high monophenolase/diphenolase activity ratio.
Conclusions
The acidic and cold-adapted tyrosinase-CNK, as a new type of tyrosinase, could expand potential applications of tyrosinases including the production of catechols through minimizing unwanted self-oxidation and the modification of existing materials at low temperature.
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Acknowledgments
This work is supported by the National Research Foundation of Korea Grant, which is funded by the Ministry of Science, ICT and Future Planning, Korea (NRF-C1ABA001-2011-0029960; to Y.S.C.), and by the Marine Biotechnology Program (Marine BioMaterials Research Center), which is funded by the Ministry of Oceans and Fisheries, Korea.
Supporting information
Supplementary Fig. 1—Multiple sequence alignment of tyrosinase-CNK and several known bacterial tyrosinases.
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Hyerin Kim and Young Joo Yeon have been equally contributed.
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Kim, H., Yeon, Y.J., Choi, Y.R. et al. A cold-adapted tyrosinase with an abnormally high monophenolase/diphenolase activity ratio originating from the marine archaeon Candidatus Nitrosopumilus koreensis . Biotechnol Lett 38, 1535–1542 (2016). https://doi.org/10.1007/s10529-016-2125-0
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DOI: https://doi.org/10.1007/s10529-016-2125-0