8. Application of tyrosinase

As an important biological resource, tyrosinase has a wide range of uses in the field of environmental engineering and many important physiological functions in the body. In addition, in combination with immobilization [75], biosensors, and other technologies, the use of tyrosinase for catalytic oxidation, treatment of industrial wastewater, and detection of compounds has gradually become a focus of research in the fields of environmental protection and biological detection.

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According to relevant studies,cistanche is a common herb that is known as "the miracle herb that prolongs life". Its main component is cistanoside, which has various effects such as antioxidant, anti-inflammatory, and immune function promotion. The mechanism between cistanche and skin whitening lies in the antioxidant effect of cistanche glycosides. Melanin in human skin is produced by the oxidation of tyrosine catalyzed by tyrosinase, and the oxidation reaction requires the participation of oxygen, so the oxygen-free radicals in the body become an important factor affecting melanin production. Cistanche contains cistanoside, which is an antioxidant and can reduce the generation of free radicals in the body, thus inhibiting melanin production.

8.1. Environmental protection 

Tyrosinase can catalyze the oxidation of mono phenolic compounds. Wada et al. [76] revealed that the rate of tyrosinase removal of substituted phenols in aqueous solutions follows the order of catechol > cresol> p-chlorophenol > phenol > pmethoxyphenol. Tyrosinase can remove not only phenols but also various organic substances such as organic amines, which eventually form a precipitate and can be easily processed. Therefore, tyrosinase in microorganisms can be used in environmental engineering fields such as factories and hospitals to degrade and treat wastewater containing phenol and amine [77]. With the continuous exploration of the treatment process, the reaction conditions have gradually been optimized. Yamada et al. found that the combination of tyrosinase and chitosan has a better effect on removing phenolic compounds in artificial wastewater. Tyrosinase catalyzes the oxidation of phenolic compounds into quinone derivatives, which are subsequently chemisorbed onto the chitosan membrane. Some alkyl-substituted phenols, such as p-methylphenol, p-propylphenol, p-butylphenol, and p-chlorophenol, have removal rates of up to 93% [78]. If the amino group of tyrosinase was fixed on the cation exchange resin, it could completely remove phenol after 2 h with hardly weakened activity for 10 cycle reuses [71]. Fixed on modified sodium aluminosilicate (NaA) and calcium aluminosilicate (CaA), tyrosinase can also be used multiple times without any decrease in activity [79]. Furthermore, the complex formed by nanomaterials and polyphenol oxidase can effectively reduce the disadvantages of traditional enzymes in treating wastewater [80].

8.2. Biological detection

Biosensor, as an emerging technology for biological detection, is an analytical device that immobilizes enzymes, DNA, antibodies, cells, etc. as molecular recognition substances on a conductor and converts chemical or thermal changes, etc. into electrical signals. It is widely used in the fields such as the food industry, environmental engineering, fermentation engineering, and medicine, because of its sensitivity, specificity, traceless, speediness, and accuracy. Wu et al. [81] quickly detected bisphenol A using nano-scale graphene as the basic tyrosinase biosensor. Yang et al. [82] developed a new tyrosine biosensor based on a chitosan carbon-coated nickel composite film, which was used to detect catechol due to the characteristics of fast, reusable, and good stability. Jiang et al. [83] by using layer-by-layer assembly technology, created an immobilized capillary tyrosinase reactor to screen for tyrosinase inhibitors. Singh et al. [84] proposed a fiber-optic biosensor based on surface plasmon resonance to detect phenolic compounds in aqueous solutions.

9. Conclusion

Because tyrosinase is involved in the process of food browning and depigmentation disorders in humans, specific probes and inhibitors have been extensively studied by researchers. Effective compounds in natural sources such as plants have the potential to inhibit tyrosinase. Using probes to detect the tyrosinase activity mechanism provides an effective means for studying the tyrosinase activity mechanism and the screening of tyrosinase inhibitors. However, the currently developed probes need to be optimized due to poor biocompatibility and stability. This article summarizes many natural, semisynthetic, and synthetic inhibitors and discusses the inhibitory effects of these compounds on the activity of tyrosinase. Based on the review, despite the wide variety of natural inhibitors, phenol-unit is still a major part of many tyrosinase inhibitors. Suitable scaffolds have been designed by many researchers based on those structures of natural compounds, but newly developed inhibitors need more effort in the future. With the development of chemical biology, more and more probes and inhibitors have better biological characteristics, which will promote our research on tyrosinase.

Declaration of competing interest

Acknowledgments

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