Tyrosinase Inhibitors from Natural and Synthetic Sources as Skin-lightening Agents

Masum, Mohammad Nuruzzaman; Yamauchi, Kosei; Mitsunaga, Tohru

doi:10.7831/ras.7.41

Cited by 67 publications

(53 citation statements)

References 81 publications

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“…Indeed, by increasing the substrate concentration from 20 µM to 200 µM, the inhibition curve shifted to the right and the IC 50 increased from 30 µM to 58 µM, demonstrating that tyrosinase inhibition by kojic acid is a competitive inhibition. This was also confirmed by other previous work in the literature [10,45]. We previously reported [27] that the degree of inhibition is equal to [I]/([I] + [IC 50 ]), which means a hyperbolic relationship exists between the degree of inhibition and concentration of an inhibitor.…”

Section: Analytical Performances Of Biosensors Based On Immobilized Tyrosinase For Inhibitor Determinationsupporting

confidence: 89%

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

Attaallah

Amine

2021

Biosensors

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An amperometric biosensor based on tyrosinase, immobilized onto a carbon black paste electrode using glutaraldehyde and BSA was constructed to detect competitive inhibitors. Three inhibitors were used in this study: benzoic acid, sodium azide, and kojic acid, and the obtained values for fifty percent of inhibition (IC50) were 119 µM, 1480 µM, and 30 µM, respectively. The type of inhibition can also be determined from the curve of the degree of inhibition by considering the shift of the inhibition curves. Amperometric experiments were performed with a biosensor polarized at the potential −0.15 V vs. Ag/AgCl and using 0.1 M phosphate buffer (pH 6.8) as an electrolyte. Under optimized conditions, the proposed biosensor showed a linear amperometric response toward catechol detection from 0.5 µM to 38 µM with a detection limit of 0.35 µM (S/N = 3), and its sensitivity was 66.5 mA M−1 cm−2. Moreover, the biosensor exhibited a good storage stability. Conversely, a novel graphical plot for the determination of reversible competitive inhibition was represented for free tyrosinase. The graph consisted of plotting the half-time reaction (t1/2) as a function of the inhibitor concentration at various substrate concentrations. This innovative method relevance was demonstrated in the case of kojic acid using a colorimetric bioassay relying on tyrosinase inhibition. The results showed that the t1/2 provides an extended linear range of tyrosinase inhibitors.

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Section: Analytical Performances Of Biosensors Based On Immobilized Tyrosinase For Inhibitor Determinationsupporting

confidence: 89%

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

Attaallah

Amine

2021

Biosensors

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“…Tyrosinase is a key enzyme which involved the catalysis of the only rate-limiting step in mammalian melanogenesis, so tyrosinase inhibitors are used to treat hyperpigmentation in the human skin [ 40 , 41 ]. As shown in Table 3 , EO showed a weak inhibitory effect on tyrosinase (IC 50 = 53.71 ± 4.89 mg/mL).…”

Section: Resultsmentioning

confidence: 99%

Chemical Composition, Antibacterial, Anti-Inflammatory, and Enzyme Inhibitory Activities of Essential Oil from Rhynchanthus beesianus Rhizome

Zhao

Chen

et al. 2020

Molecules

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Rhynchanthus beesianus W. W. Smith, an edible, medicinal, and ornamental plant, is mainly cultivated in China and Myanmar. The essential oil (EO) from R. beesianus rhizome has been used as an aromatic stomachic in China. The chemical composition and biological activities of EO from R. beesianus rhizome were reported for the first time. Based on gas chromatography with flame ionization or mass selective detection (GC-FID/MS) results, the major constituents of EO were 1,8-cineole (47.6%), borneol (15.0%), methyleugenol (11.2%), and bornyl formate (7.6%). For bioactivities, EO showed a significant antibacterial activity against Staphylococcus aureus, Enterococcus faecalis, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa, and Proteus vulgaris with the diameter of the inhibition zone (DIZ) (8.66–10.56 mm), minimal inhibitory concentration (MIC) (3.13–6.25 mg/mL), and minimal bactericidal concentration (MBC) (6.25–12.5 mg/mL). Moreover, EO (128 μg/mL) significantly inhibited the production of proinflammatory mediators nitric oxide (NO) (92.73 ± 1.50%) and cytokines tumor necrosis factor-α (TNF-α) (20.29 ± 0.17%) and interleukin-6 (IL-6) (61.08 ± 0.13%) in lipopolysaccharide (LPS)-induced RAW264.7 macrophages without any cytotoxic effect. Moreover, EO exhibited significant acetylcholinesterase (AChE) inhibitory activity (the concentration of the sample that affords a 50% inhibition in the assay (IC50) = 1.03 ± 0.18 mg/mL) and moderate α-glucosidase inhibition effect (IC50 = 11.60 ± 0.25 mg/mL). Thus, the EO could be regarded as a bioactive natural product and has a high exploitation potential in the cosmetics and pharmaceutical industries.

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“…Melanin is a widespread natural pigment that is responsible for color in hair, skin, and eyes. It provides protection against the deleterious effects of ultraviolet (UV) irradiation [1]. Melanogenesis is the physiological process of melanin formation in which TYR, a copper-dependent enzyme, initiates the first step.…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase and Melanogenesis Inhibition by Indigenous African Plants: A Review

et al. 2020

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The indiscriminate use of non-regulated skin lighteners among African populations has raised health concerns due to the negative effects associated with skin lightener toxicity. For this reason, there is a growing interest in the cosmetic development of plants and their metabolites as alternatives to available chemical-derived skin lightening formulations. Approximately 90% of Africa’s population depends on traditional medicine, and the continent’s biodiversity holds plant material with various biological activities, thus attracting considerable research interest. This study aimed to review existing evidence and document indigenous African plant species capable of inhibiting the enzyme tyrosinase and melanogenesis for potential incorporation into skin lightening products. Literature search on melanin biosynthesis, skin lightening, and tyrosinase inhibitors resulted in the identification of 35 plant species were distributed among 31 genera and 21 families across 15 African countries and 9 South African provinces. All plants identified in this study showed competent tyrosinase and melanogenesis inhibitory capabilities. These results indicate that African plants have the potential to serve as alternatives to current chemically-derived skin lighteners.

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Tyrosinase Inhibitors from Natural and Synthetic Sources as Skin-lightening Agents

Cited by 67 publications

References 81 publications

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

The Kinetic and Analytical Aspects of Enzyme Competitive Inhibition: Sensing of Tyrosinase Inhibitors

Chemical Composition, Antibacterial, Anti-Inflammatory, and Enzyme Inhibitory Activities of Essential Oil from Rhynchanthus beesianus Rhizome

Tyrosinase and Melanogenesis Inhibition by Indigenous African Plants: A Review

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