Spectrophotometric Assays for Sensing Tyrosinase Activity and Their Applications

Abstract

Tyrosinase (TYR, E.C. 1.14.18.1), a critical enzyme participating in melanogenesis, catalyzes the first two steps in melanin biosynthesis including the ortho-hydroxylation of L-tyrosine and the oxidation of L-DOPA. Previous pharmacological investigations have revealed that an abnormal level of TYR is tightly associated with various dermatoses, including albinism, age spots, and malignant melanoma. TYR inhibitors can partially block the formation of pigment, which are always used for improving skin tone and treating dermatoses. The practical and reliable assays for monitoring TYR activity levels are very useful for both disease diagnosis and drug discovery. This review comprehensively summarizes structural and enzymatic characteristics, catalytic mechanism and substrate preference of TYR, as well as the recent advances in biochemical assays for sensing TYR activity and their biomedical applications. The design strategies of various TYR substrates, alongside with several lists of all reported biochemical assays for sensing TYR including analytical conditions and kinetic parameters, are presented for the first time. Additionally, the biomedical applications and future perspectives of these optical assays are also highlighted. The information and knowledge presented in this review offer a group of practical and reliable assays and imaging tools for sensing TYR activities in complex biological systems, which strongly facilitates high-throughput screening TYR inhibitors and further investigations on the relevance of TYR to human diseases.

Cosmeceutical Potential of Extracts Derived from Fishery Industry Residues: Sardine Wastes and Codfish Frames

“…However, these winery residues extracts presented higher tyrosinase (IC 50 from 4.0 to 0.14 mg extract/mL) and elastase (IC 50 from 3.4 to 0.1 mg extract/mL) inhibitory capacities than those obtained in this work, probably due to the presence of phenolic compounds that are recognized to have several bioactivities. It is important to mention that in our study we used mushroom tyrosinase to screen the anti-hyperpigmentation effect of extracts, as this enzyme has been widely used in high throughput assays [ 37 ]. Nevertheless, since there are some controversies regarding the similarity and homology of this enzyme with mammalian/human tyrosinase [ 38 , 39 , 40 ], future studies involving mammalian cell lines should be considered to evaluate the potential anti-hyperpigmentation effect of sardine and codfish extracts.…”

Recent Advances in the Development of Oxidoreductase-Based Biosensors for Detection of Phenolic Antioxidants in Food and Beverages

“…On the other hand, in the diphenolase cycle which involves the oxidation of o -diphenols to o -quinones, E oxy continues to bind o -diphenol (E oxy D complex), while both E met and E oxy have the ability to catalyze the oxidation of the bound diphenol to its corresponding o -quinone. Following that, E met is regenerated to complete the enzymatic cycle …”

“…Following that, E met is regenerated to complete the enzymatic cycle. 18 Biosensors containing tyrosinase have been employed to monitor various phenolic antioxidants viz., tyrosol, catechin, and gallic acid among others. 9,19 Cerrato-Alvarez et al 9 prepared a tyrosinase-based electrochemical biosensor for sensing phenolic antioxidants present in beer.…”

Self-assembled peptides-modified flexible field-effect transistors for tyrosinase detection

“…The detection of tyrosinase is, therefore, crucial for practical clinical diagnosis and prognosis. Several laboratory-based methodologies have been developed for detecting tyrosinase activity, including fluorometry, colorimetry, spectrophotometry, electrochemistry ( Zhan et al., 2018 ; Liu et al., 2013 , 2017 ; Ciui et al., 2018 ; Fan et al., 2021 ).…”