A perspective on the biotechnological applications of the versatile tyrosinase. (October 2019)

• Record Type: Journal Article
• Authors: Min, Kyoungseon; Park, Gwon Woo; Yoo, Young Je; Lee, Jin-Suk
• Is Part Of: Bioresource technology. Volume 289(2019)
• Publication Date: 2019-10
• Subjects: Tyrosinase -- Versatility -- Industrial application; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2019.121730
• Languages: English
• ISSNs: 0960-8524

Abstract

Highlights: Tyrosinase is bifunctional Cu-containing oxidoreductase for diverse phenolic compounds. Tyrosinase is conventionally applicable for bioremediation and biosensor construction. In addition, tyrosinase has been used for L-DOPA synthesis (e.g. electroenzymatic system). Recently, it is reported to promiscuous activity of tyrosinase for delignification. This review focuses on new perspective of tyrosinase for industrial applications. Abstract: Tyrosinase (E.C. 1.14.18. 1) is a type of Cu-containing oxidoreductase which has bifunctional activity for various phenolic substrates: ortho -hydroxylation of monophenols to diphenols (a cresolase activity) and oxidation of diphenols to quinones (a catecholase activity). Based on the broad substrate spectrum, tyrosinase has been used in bioremediation of phenolic pollutants, constructing biosensors for identifying phenolic compounds, and L-DOPA synthesis. Furthermore, not only tyrosinase has been used to produce useful polyphenol derivatives, but also it is recently revealed that the promiscuous activity of tyrosinase is closely related with delignification in the biorefinery. Accordingly, tyrosinase might be a potential biocatalyst for industrial applications (e.g., electroenzymatic L-DOPA production, but its long-term stability and reusability should be further explored. In this review, we emphasize the versatility of tyrosinase, which includes conventional applications, and suggest new perspectives as an industrial biocatalyst (e.g., electroenzymatic L-DOPA production). Especially, this review focuses on and comprehensively discusses recent innovative studies.