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Journal articles on the topic 'Tyrosinase activity'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Suwunwong, T., T. Kobkeatthawin, K. Chanawanno, N. Saewan, P. Wisitsak, and Suchada Chantrapromma. "Tyrosinase Inhibitory Activity of Pyrazole Derivatives." Advanced Materials Research 506 (April 2012): 194–97. http://dx.doi.org/10.4028/www.scientific.net/amr.506.194.

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A series of 3,5-substituted-4,5-dihydro-1H-pyrazole-1-carbothioamide derivatives were synthesized. Their structures were determined on the basis of spectroscopic data interpretation and their tyrosinase inhibitory activity was determined. The results showed that compound 2 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 91.866 ± 2.086 with L-tyrosine as substrate whereas compound 3 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 79.266 ± 0.552 and 89.593 ± 1.015 with L-tyrosine and L-DOPA as substrates. The IC50v

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2

Kwak, Jung-Hoon, and Yeong-Hwan Han. "Tyrosinase Inhibitory Activity of Macrolepiota procera." Korean Journal of Mycology 38, no. 2 (2010): 202–4. http://dx.doi.org/10.4489/kjm.2010.38.2.202.

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3

Lopez-Tejedor, David, Rafael Claveria-Gimeno, Adrian Velazquez-Campoy, Olga Abian, and Jose M. Palomo. "In Vitro Antiviral Activity of Tyrosinase from Mushroom Agaricus bisporus against Hepatitis C Virus." Pharmaceuticals 14, no. 8 (2021): 759. http://dx.doi.org/10.3390/ph14080759.

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Tyrosinases from a commercial Agaricus bisporus protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from A. bisporus (TyrAB) of 45 kDa and a newly discovered 50 kDa tyrosinase isoform (Tyr50 kDa), and tested showing high antiviral activity against the hepatitis C virus for the first time. Cell toxicity and antiviral activity of tyrosinases were determined in cultured Huh 5-2 liver tumor cells transfected with a replicon system (a plasmid that includes all non-structural hepatitis C virus proteins and replicates autonomously).

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4

Lee, Sanggwon, Heejeong Choi, Yujin Park, et al. "Urolithin and Reduced Urolithin Derivatives as Potent Inhibitors of Tyrosinase and Melanogenesis: Importance of the 4-Substituted Resorcinol Moiety." International Journal of Molecular Sciences 22, no. 11 (2021): 5616. http://dx.doi.org/10.3390/ijms22115616.

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We previously reported (E)-β-phenyl-α,β-unsaturated carbonyl scaffold ((E)-PUSC) played an important role in showing high tyrosinase inhibitory activity and that derivatives with a 4-substituted resorcinol moiety as the β-phenyl group of the scaffold resulted in the greatest tyrosinase inhibitory activity. To examine whether the 4-substituted resorcinol moiety could impart tyrosinase inhibitory activity in the absence of the α,β-unsaturated carbonyl moiety of the (E)-PUSC scaffold, 10 urolithin derivatives were synthesized. To obtain more candidate samples, the lactone ring in synthesized urol

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5

Schallreuter-Wood, Karin U., and John M. Wood. "Control of Melanogenesis In the Human Epidermis by the Redox-Status of Tetrahydrobiopterins." Pteridines 6, no. 3 (1995): 101–3. http://dx.doi.org/10.1515/pteridines.1995.6.3.101.

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Summary Activity of tyrosinase directly controls melanogenesis in the human epidermis. Recently, it has been shown that the biosynthesis and recycling of (6R)L-erythro 5,6,7,8 tetrahydrobiopterin (6-BH4) plays a central role in regulating the supply of L-tyrosine, the substrate for tyrosinase. In this report, we present evidence that 6-BH4 and other tetrahydropterins, have the capacity to regulate tyrosinase activity directly by a specific uncompetitive mechanism. This fine control of tyrosinase activity/melanogenesis in the human epiidermis depends on the redox equilibrium 6-BH4 ↔ dihydropter

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6

Song, Hanbit, Pyung-Gang Lee, Hyun Kim, et al. "Polyphenol-Hydroxylating Tyrosinase Activity under Acidic pH Enables Efficient Synthesis of Plant Catechols and Gallols." Microorganisms 9, no. 9 (2021): 1866. http://dx.doi.org/10.3390/microorganisms9091866.

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Tyrosinase is generally known as a melanin-forming enzyme, facilitating monooxygenation of phenols, oxidation of catechols into quinones, and finally generating biological melanin. As a homologous form of tyrosinase in plants, plant polyphenol oxidases perform the same oxidation reactions specifically toward plant polyphenols. Recent studies reported synthetic strategies for large scale preparation of hydroxylated plant polyphenols, using bacterial tyrosinases rather than plant polyphenol oxidase or other monooxygenases, by leveraging its robust monophenolase activity and broad substrate speci

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7

Xiu-Hua, Jia, Lin Shao-Chun, Huang Bing, et al. "Tyrosinase Small Interfering RNA Effectively Suppresses Tyrosinase Gene Expression In Vitro and In Vivo." Molecular Biology International 2010 (November 4, 2010): 1–6. http://dx.doi.org/10.4061/2010/240472.

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Tyrosinase is a bifunctional enzyme which oxidizes the initial step of melanin biosynthesis, that is, conversion of tyrosine to dopa and subsequently dopa to dopaquinone. It is a glycosylated protein and a major regulator of melanogenesis. To date, many approaches have been tried to regulate tyrosinase activity and melanin content. To that end, we screened small interfering RNA sequences for sequence-inhibited tyrosinase expression in B16 cells and in C57BL/6 mice. We analyzed tyrosinase mRNA levels by quantitative real-time PCR and determined tyrosinase activity and melanin content at 24, 48,

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8

Pintus, Francesca, Delia Spanò, Angela Corona, and Rosaria Medda. "Antityrosinase activity ofEuphorbia characiasextracts." PeerJ 3 (October 13, 2015): e1305. http://dx.doi.org/10.7717/peerj.1305.

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Tyrosinase is a well-known key enzyme in melanin biosynthesis and its inhibitors have become increasingly important because of their potential use as hypopigmenting agents. In the present study, the anti-melanogenic effect of aqueous and ethanolic extracts fromEuphorbia characiasleaves, stems, and flowers in cell-free and cellular systems was examined. All the extracts showed inhibitory effects against mushroom tyrosinase with leaf extracts exhibiting the lowest IC50values of 24 and 97 µg/mL for aqueous and ethanolic extracts respectively. Enzyme kinetic analysis indicated that leaf aqueous ex

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9

Manandhar, Wagle, Seong, et al. "Phlorotannins with Potential Anti-tyrosinase and Antioxidant Activity Isolated from the Marine Seaweed Ecklonia stolonifera." Antioxidants 8, no. 8 (2019): 240. http://dx.doi.org/10.3390/antiox8080240.

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Compounds were isolated from Ecklonia stolonifera Okamura, a marine brown alga widely consumed as food. Among the isolated compounds, 974-A was demonstrated for the first time to be a potent competitive inhibitor of mushroom tyrosinase activity towards l-tyrosine and l-DOPA (IC50 values = 1.57 ± 0.08 and 3.56 ± 0.22 µM, respectively). Molecular docking simulations clarified that the hydroxyl residues of the isolated compounds formed hydrogen bonds with residues at the catalytic and allosteric sites of tyrosinase, while other residues participated in hydrophobic interactions. Moreover, 974-A, p

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10

OLIVARES, Concepción, Celia JIMÉNEZ-CERVANTES, José Antonio LOZANO, Francisco SOLANO, and José Carlos GARCÍA-BORRÓN. "The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase." Biochemical Journal 354, no. 1 (2001): 131–39. http://dx.doi.org/10.1042/bj3540131.

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Melanin synthesis in mammals is catalysed by at least three enzymic proteins, tyrosinase (monophenol dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) and tyrosinase-related proteins (tyrps) 1 and 2, whose genes map to the albino, brown and slaty loci in mice, respectively. Tyrosinase catalyses the rate-limiting generation of l-dopaquinone from l-tyrosine and is also able to oxidize l-dopa to l-dopaquinone. Conversely, mouse tyrp1, but not tyrosinase, catalyses the oxidation of the indolic intermediate 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into the corresponding 5,6-indolequi

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11

Kubo, Isao, Qing-Xi Chen, Ken-Ichi Nihei, José S. Calderón, and Carlos L. Céspedes. "Tyrosinase Inhibition Kinetics of Anisic Acid." Zeitschrift für Naturforschung C 58, no. 9-10 (2003): 713–18. http://dx.doi.org/10.1515/znc-2003-9-1021.

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AbstractAnisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from aniseed, a common food spice. It inhibited the oxidation of l-3,4-dihydroxyphenylalanine (ʟ- DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mᴍ. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive inhibitor and the inhibition constant KI was obtained as 0.603 mᴍ. Anisic acid also inhibited the hydroxylation of ʟ-tyrosine catalyzed by tyrosinase. The lag phase caused by the monophenolase acti

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12

Kurihara, Hideyuki, and Kazuki Kujira. "Phlorotannins Derived From the Brown Alga Colpomenia bullosa as Tyrosinase Inhibitors." Natural Product Communications 16, no. 7 (2021): 1934578X2110213. http://dx.doi.org/10.1177/1934578x211021317.

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Tyrosinase catalyzes hydroxylation of L-tyrosine and dehydrogenation of L-DOPA in the melanin biosynthesis pathway. Tyrosinase inhibitors have potential use as cosmetic whitening agents and for preventing seafood deterioration. In this report, tyrosinase inhibitors extracted from brown alga Colpomenia bullosa (Scytosiphonaceae, Scytosiphonales) were investigated. Inhibitory principles were isolated from the extract and identified as phlorotannins, phloroglucinol (1), diphlorethol (2), triphlorethol C (3), which have not been isolated in a free form previously, and fucophlorethol C (4). Compoun

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13

Boyek, Rodney F., David P. Mascotti, and Schori Barbara E. "Ferroxidase activity of mushroom tyrosinase." Phytochemistry 25, no. 6 (1986): 1281–83. http://dx.doi.org/10.1016/s0031-9422(00)81272-8.

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14

Yang, Zhen, and Donald A. Robb. "Tyrosinase activity in reversed micelles." Biocatalysis and Biotransformation 23, no. 6 (2005): 423–30. http://dx.doi.org/10.1080/10242420500387433.

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15

Hałdys, Katarzyna, and Rafał Latajka. "Thiosemicarbazones with tyrosinase inhibitory activity." MedChemComm 10, no. 3 (2019): 378–89. http://dx.doi.org/10.1039/c9md00005d.

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16

Yang, Zhen, Ya-Jun Yue, and Miao Xing. "Tyrosinase activity in ionic liquids." Biotechnology Letters 30, no. 1 (2007): 153–58. http://dx.doi.org/10.1007/s10529-007-9505-4.

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17

Miranda, Michele, Antonella Bonfigli, Osvaldo Zarivi, Anna Maria Ragnelli, Giovanni Pacioni, and Dario Botti. "Truffle tyrosinase: Properties and activity." Plant Science 81, no. 2 (1992): 175–82. http://dx.doi.org/10.1016/0168-9452(92)90040-s.

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18

Li, Qi, Hongyu Yang, Jun Mo, et al. "Identification by shape-based virtual screening and evaluation of new tyrosinase inhibitors." PeerJ 6 (January 26, 2018): e4206. http://dx.doi.org/10.7717/peerj.4206.

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Targeting tyrosinase is considered to be an effective way to control the production of melanin. Tyrosinase inhibitor is anticipated to provide new therapy to prevent skin pigmentation, melanoma and neurodegenerative diseases. Herein, we report our results in identifying new tyrosinase inhibitors. The shape-based virtual screening was performed to discover new tyrosinase inhibitors. Thirteen potential hits derived from virtual screening were tested by biological determinations. Compound 5186-0429 exhibited the most potent inhibitory activity. It dose-dependently inhibited the activity of tyrosi

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19

Slominski, A., G. Moellmann, and E. Kuklinska. "MSH inhibits growth in a line of amelanotic hamster melanoma cells and induces increases in cyclic AMP levels and tyrosinase activity without inducing melanogenesis." Journal of Cell Science 92, no. 4 (1989): 551–59. http://dx.doi.org/10.1242/jcs.92.4.551.

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In Bomirski Ab amelanotic hamster melanoma cells, L-tyrosine and/or L-dopa induce increases in tyrosinase activity as well as synthesis of melanosomes and melanin. L-tyrosine also modifies melanocyte-stimulating hormone (MSH) binding. In this paper we show that in the Bomirski amelanotic melanoma system MSH and agents that raise intracellular cyclic AMP induce dendrite formation, inhibit cell growth, and cause substantial increases in tyrosinase activity without inducing melanin synthesis. Tyrosinase activity is detected only in broken cell preparations, or cytochemically in fixed cells. In th

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20

MATEE, Lusanda P., Richard P. BECKETT, Knut A. SOLHAUG, and Farida V. MINIBAYEVA. "Characterization and role of tyrosinases in the lichenLobaria pulmonaria(L.) Hoffm." Lichenologist 48, no. 4 (2016): 311–22. http://dx.doi.org/10.1017/s0024282916000293.

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AbstractTyrosinases are a widespread family of multicopper oxidase enzymes. In our earlier work, we identified the presence of tyrosinases in lichenized Ascomycetes based on their substratum specificity, sensitivity to inhibitors and molecular mass. Here, we present a more detailed characterization of a tyrosinase from the lichenLobaria pulmonaria. We also compare tyrosinase activity with the activities of laccases and peroxidases, the other redox enzymes present in this species. The importance of tyrosinases in lichen biology was studied by testing their role in melanin synthesis. Laboratory

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21

Purnamasari, Dini Rizky. "TEST OF TYROSINASE ENZYME INHIBITOR ACTIVITY OF BIDARA ARAB LEAVES ETHANOL EXTRACT (ZIZIPHUS SPINA-CHRISTI L.) BY IN VITRO." INDONESIA NATURAL RESEARCH PHARMACEUTICAL JOURNAL 5, no. 1 (2020): 35–44. http://dx.doi.org/10.52447/inspj.v5i1.1739.

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Bidara Arab (Ziziphus spina-christi L.) is one of the tropical trees that is very useful and is often called a versatile plant. Several studies have proven that this plant is used as an antimicrobial, antidiabetic, antipireutic, anticancer and also has the potential to inhibit the enzyme tyrosinase. Kojic acid is one of the agents used to inhibit the tyrosinase enzyme so that it prevents hyperpigmentation. This study aims to determine the inhibitory activity of the tyrosinase enzyme from the ethanol extract of Bidara Arab leaves (Ziziphus spina-christi L.) in vitro. The method used in extracti

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22

Kim, Chang, Sang Noh, Yujin Park та ін. "A Potent Tyrosinase Inhibitor, (E)-3-(2,4-Dihydroxyphenyl)-1-(thiophen-2-yl)prop-2-en-1-one, with Anti-Melanogenesis Properties in α-MSH and IBMX-Induced B16F10 Melanoma Cells". Molecules 23, № 10 (2018): 2725. http://dx.doi.org/10.3390/molecules23102725.

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In this study, we designed and synthesized eight thiophene chalcone derivatives (1a–h) as tyrosinase inhibitors and evaluated their mushroom tyrosinase inhibitory activities. Of these eight compounds, (E)-3-(2,4-dihydroxyphenyl)-1-(thiophen-2-yl)prop-2-en-1-one (1c) showed strong competitive inhibition activity against mushroom tyrosinase with IC50 values of 0.013 μM for tyrosine hydroxylase and 0.93 μM for dopa oxidase. In addition, we used enzyme kinetics study and docking program to further evaluate the inhibitory mechanism of 1c toward tyrosinase. As an underlying mechanism of 1c mediated

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23

Paudel, Pradeep, Aditi Wagle, Su Hui Seong, Hye Jin Park, Hyun Ah Jung, and Jae Sue Choi. "A New Tyrosinase Inhibitor from the Red Alga Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae)." Marine Drugs 17, no. 5 (2019): 295. http://dx.doi.org/10.3390/md17050295.

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A marine red alga, Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae), is a rich source of bromophenols with a wide array of biological activities. This study investigates the anti-tyrosinase activity of the alga. Moderate activity was demonstrated by the methanol extract of S. latiuscula, and subsequent column chromatography identified three bromophenols: 2,3,6-tribromo-4,5-dihydroxybenzyl methyl alcohol (1), 2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether (2), and bis-(2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether) (3). Bromophenols 1 and 3 exhibited potent competitive tyrosinase inh

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24

Naish-Byfield, S., and P. A. Riley. "Oxidation of monohydric phenol substrates by tyrosinase. An oximetric study." Biochemical Journal 288, no. 1 (1992): 63–67. http://dx.doi.org/10.1042/bj2880063.

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The purity of commercially available mushroom tyrosinase was investigated by non-denaturing PAGE. Most of the protein in the preparation migrated as a single band under these conditions. This band contained both tyrosinase and dopa oxidase activity. No other activity of either classification was found in the preparation. Oxygen consumption by tyrosinase during oxidation of the monohydric phenol substrates tyrosine and 4-hydroxyanisole (4HA) was monitored by oximetry in order to determine the stoichiometry of the reactions. For complete oxidation, the molar ratio of oxygen: 4HA was 1:1. Under i

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Lee, Na Young. "Antioxidant Effect and Tyrosinase Inhibition Activity of Seaweeds Ethanol Extracts." Journal of the Korean Society of Food Science and Nutrition 42, no. 12 (2013): 1893–98. http://dx.doi.org/10.3746/jkfn.2013.42.12.1893.

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26

Park, Hee-Young, Jesus Perez, Richard Laursen, and Barbara A. Gilchrest. "A tyrosinase mimetic peptide inhibits tyrosinase activity in cultured human melanocytes." Journal of Dermatological Science 16 (March 1998): S134. http://dx.doi.org/10.1016/s0923-1811(98)83797-3.

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27

Micillo, Raffaella, Julia Sirés-Campos, José García-Borrón, Lucia Panzella, Alessandra Napolitano, and Conchi Olivares. "Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase." International Journal of Molecular Sciences 19, no. 8 (2018): 2156. http://dx.doi.org/10.3390/ijms19082156.

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Caffeic acid derivatives represent promising lead compounds in the search for tyrosinase inhibitors to be used in the treatment of skin local hyperpigmentation associated to an overproduction or accumulation of melanin. We recently reported the marked inhibitory activity of a conjugate of caffeic acid with dihydrolipoic acid, 2-S-lipoylcaffeic acid (LCA), on the tyrosine hydroxylase (TH) and dopa oxidase (DO) activities of mushroom tyrosinase. In the present study, we evaluated a more lipophilic derivative, 2-S-lipoyl caffeic acid methyl ester (LCAME), as an inhibitor of tyrosinase from human

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Chochkova, Maya, Assya Georgieva, Galya Ivanova, et al. "Synthesis and biological activity of hydroxycinnamoyl containing antiviral drugs." Journal of the Serbian Chemical Society 79, no. 5 (2014): 517–26. http://dx.doi.org/10.2298/jsc130222103c.

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Seven N-hydroxycinnamoyl amides were synthesized by EDC/HOBt coupling of the corresponding substituted cinnamic acids (p-coumaric-, ferulic-, sinapic- and caffeic acids) with influenza antivirals (amantadine, rimantadine and oseltamivir). DPPH (1,1-diphenyl-2-picrylhydrazyl) scavenging abilities and the inhibitory effect on mushroom tyrosinase activity (using L-tyrosine as the substrate) were investigated in vitro. Amongst the synthesized compounds, N-[(E)-3-(3?,4?-dihydroxyphenyl)-2-propenoyl]oseltamivir (1) and N-[(E)-3-(3?,4?-dihydroxyphenyl)-2-propenoyl]rimantadine (4), containing catechol

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Halaban, Ruth, Elaine Cheng, Sherri Svedine, Rebecca Aron, and Daniel N. Hebert. "Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine." Journal of Biological Chemistry 276, no. 15 (2000): 11933–38. http://dx.doi.org/10.1074/jbc.m008703200.

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Tyrosinase is essential for pigmentation and is a source of tumor-derived antigenic peptides and cellular immune response. Wild type tyrosinase in melanoma cells and certain albino mutants in untransformed melanocytes are targeted to proteolytic degradation by the 26 S proteasome due to retention of the misfolded protein in the endoplasmic reticulum and its subsequent retranslocation to the cytosol. Here, we demonstrate that the substrates DOPA and tyrosine induced in melanoma cells a transition of misfolded wild type tyrosinase to the native form that is resistant to proteolysis, competent to

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Puspaningtyas, Ayik Rosita. "Evaluation of the effect of red guava (Psidium guajava) fruit extract on tyrosinase (EC 1.14.18.1) activity by spectrophotometry." International Current Pharmaceutical Journal 1, no. 5 (2012): 92–97. http://dx.doi.org/10.3329/icpj.v1i5.10280.

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Tyrosinase is one of the most important enzymes in melanin biosynthesis. Inhibition of tyrosinase activity will cause a decrease in melanin production. Tyrosinase inhibitory activity by ascorbic acid has been studied before. Based on reported experiments, ascorbic acid can inhibit tyrosinase activity in enzymatic reaction competitively. As an effort to find out a skin whitening agent which is effective, safe and have minimum adverse effect, the inhibitory activities of Psidium guajava extract was studied on tyrosinase activity. This is one of the fruits that contains high amount of ascorbic ac

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Batubara, Irmanida, Maily Mustofa, Wulan Tri Wahyuni, et al. "Tyrosinase Inhibition, Antiglycation, and Antioxidant Activity of Xylocarpus granatum." Biosaintifika: Journal of Biology & Biology Education 12, no. 1 (2020): 70–75. http://dx.doi.org/10.15294/biosaintifika.v12i1.22676.

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Xylocarpus granatum is mangrove plant that traditionally used as face powder in Central Sulawesi, Indonesia which related to antioxidant, antiglycation and tyrosinase inhibition activities. This study aimed to evaluate the potency of X. granatum as a tyrosinase inhibitor, antiglycation, and antioxidant. The leaves, stem, stem bark, fruit flesh, fruit peel, and kernel of X. granatum were extracted using ethanol then their tyrosinase inhibition, antiglycation, and antioxidant were evaluated. Tyrosinase inhibition activity was evaluated using in vitro assay with L-tyrosine and L-DOPA as the subst

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Sagala, Zuraida, and Kurnia Telaumbanua. "FORMULATION, STABILTY TEST AND ENZYME ACTIVITY TEST TYROSINASE OF CREAM PEPARATIONS FROM HERENDONG FRUIT EXTRACT(Melastoma affine D. Don)." INDONESIA NATURAL RESEARCH PHARMACEUTICAL JOURNAL 5, no. 2 (2020): 149–73. http://dx.doi.org/10.52447/inspj.v5i2.4451.

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One way to prevent or inhibit melanin formation is by inhibiting tyrosinase activity (Lloyd,2011). Tyrosinase enzyme is an enzyme that plays a role in the formation of skin pigments or known as melanogenesis. In the process of melanogenesis, the enzyme tyrosinase acts as a catalyst in two different reactions, namely the hydroxylation process of tyrosine to dihydroxy-phenylalanine (L-DOPA) and oxidation of L-DOPA to quinone DOPA. Tyrosinase in skin tissue is activated by solar UV radiation so that it accelerates the process of melanin production (Fais et al. 2009). This study was conducted to d

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Nursid, Muhamad, Endar Marraskuranto, Dilaika Septorini, and Irmanida Batubara. "Screening of Marine-Derived Fungi Extracts as Antioxidant, Tyrosinase Inhibitor, and Antiglycation." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 14, no. 1 (2019): 33. http://dx.doi.org/10.15578/squalen.v14i1.366.

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Marine-derived fungi are of great interest as new promising sources of bioactive secondary metabolites. The aim of this study was to determine the antioxidant activity, tyrosinase inhibitor and antiglycation of marine-derrived fungi collected from Kepulauan Seribu Marine National Park, Indonesia. Antioxidant screening was determined using the 1,1-diphenyl-2-picryl hydrazyl (DPPH) method. The tyrosinase inhibitor was screened using L-tyrosine substrate, while the antiglycation test was determined by the ability to inhibit the formation of advanced glycation end products (AGEs). A total of 28 ma

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Schurink, Marloes, Willem J. H. van Berkel, Harry J. Wichers, and Carmen G. Boeriu. "Novel peptides with tyrosinase inhibitory activity." Peptides 28, no. 3 (2007): 485–95. http://dx.doi.org/10.1016/j.peptides.2006.11.023.

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35

Tomšovský, M., and L. Homolka. "Tyrosinase Activity Discovered in Trametes spp." World Journal of Microbiology and Biotechnology 20, no. 5 (2004): 529–30. http://dx.doi.org/10.1023/b:wibi.0000040404.83282.5c.

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No, Jae Kyung, Min Sun Kim, You Jung Kim, Song Ja Bae, Jae Sue Choi, and Hae Young Chung. "Inhibition of Tyrosinase by Protocatechuic Aldehyde." American Journal of Chinese Medicine 32, no. 01 (2004): 97–103. http://dx.doi.org/10.1142/s0192415x04001801.

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The purpose of this study was to determine the inhibitory action of protocatechuic aldehyde (PCA) on tyrosinase activity. PCA is one of the compounds found in the root of Salvia miltiorrhiza. Our study documented that PCA has a potent inhibitory effect on tyrosinase, which catalyzes the rate-limiting step of melanin biosynthesis. Although melanin biosynthesis has an essential function normally in human skin for defense against ultraviolet light of the sun, its abnormal activity as seen in pigmentation disorder could lead to serious medical problems. Our data showed that PCA, with concentration

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Tripathi, R. K., C. Chaya Devi, and A. Ramaiah. "pH-dependent interconversion of two forms of tyrosinase in human skin." Biochemical Journal 252, no. 2 (1988): 481–87. http://dx.doi.org/10.1042/bj2520481.

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1. We have shown that the characteristic lag in cresolase activity of human skin tyrosinase at inhibitory concentration of tyrosine was absent at all pH values studied, i.e. pH 5.2, 5.7, 6.2 and 6.8, if the enzyme solubilized at low pH was used as the source of enzyme, but the same enzyme when dialysed against buffers of various pH values showed linear activity only at pH 5.2 and was not inhibited by excess tyrosine, whereas at higher pH values it exhibited a lag and inhibition by excess tyrosine. 2. However, the enzyme solubilized in buffer/detergent, pH 6.8, when dialysed against buffer of t

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38

Park, Jisu, Hyejung Jung, Kyuri Kim, et al. "D-tyrosine negatively regulates melanin synthesis by competitively inhibiting tyrosinase activity." Pigment Cell & Melanoma Research 31, no. 3 (2017): 374–83. http://dx.doi.org/10.1111/pcmr.12668.

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39

Andrawis, A., and V. Kahn. "Effect of methimazole on the activity of mushroom tyrosinase." Biochemical Journal 235, no. 1 (1986): 91–96. http://dx.doi.org/10.1042/bj2350091.

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Methimazole (1-methyl-2-mercaptoimidazole) inhibits both the mono- and the o-dihydroxyphenolase activities of mushroom tyrosinase when assayed spectrophotometrically. With DL-3,4-dihydroxyphenylalanine as substrate, the inhibition was found to be a mixed-type one with Ki 4.6 × 10(-6) M. We found that methimazole can interact with the oxidation products of o-dihydroxyphenols, probably with o-quinones, to form a conjugate. The conjugate formed between methimazole and o-benzoquinone was separated by chromatography on Sephadex G-10 and was characterized by an absorption maximum at 248-260 nm. Our

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40

Winder, A. J., A. Wittbjer, E. Rosengren, and H. Rorsman. "Fibroblasts expressing mouse c locus tyrosinase produce an authentic enzyme and synthesize phaeomelanin." Journal of Cell Science 104, no. 2 (1993): 467–75. http://dx.doi.org/10.1242/jcs.104.2.467.

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Recent advances in the study of the molecular biology of mouse pigmentation have led to the discovery of a family of proteins involved in the control of melanin synthesis. It has been confirmed that the product of the mouse c (albino) locus is the key melanogenic enzyme tyrosinase, but study of its function and regulation have been hampered by the presence of closely related proteins within melanin-synthesising cells. To overcome these problems, we have established lines of mouse fibroblasts expressing the c locus mouse tyrosinase. Here we describe characterisation of the tyrosinase synthesise

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Suzu, Ikuko, Hiroki Goto, Nami Hiwatashi, et al. "Antioxidant and Antityrosinase Activity of Cissus quadrangularis Extract." Natural Product Communications 8, no. 5 (2013): 1934578X1300800. http://dx.doi.org/10.1177/1934578x1300800522.

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The effects of Cissus quadrangularis Linn. extract on antioxidation and tyrosinase inhibition were investigated. The extract showed anti-oxidative activity with an IC50 value of 522.0 μg/mL, and inhibitory effects on tyrosinase activity and melanin production in B16 melanocytes in a dose-dependent manner (100-2000 μg/mL). This study suggests that this species contains anti-tyrosinase components.

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42

Sun, Biyun, A. Daryl Ariawan, Holly Warren, et al. "Programmable enzymatic oxidation of tyrosine–lysine tetrapeptides." Journal of Materials Chemistry B 8, no. 15 (2020): 3104–12. http://dx.doi.org/10.1039/d0tb00250j.

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Fmoc-capped tetrapeptides bearing two lysines and two tyrosines show programmable enzymatic activity. Solvent accessible tyrosines determine the extent of reactivity with tyrosinase, and subsequent quinone formation drives polymerisation.

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43

Heo, Da-Jeong, Su-Jung Kim, Ae-Ran Choi, Hae-Ryong Park, and Seung-Cheol Lee. "Tyrosinase Inhibitory Activity and Neuronal Cell Protection of Hydrothermal Extracts from Watermelons." Journal of the Korean Society of Food Science and Nutrition 42, no. 10 (2013): 1707–11. http://dx.doi.org/10.3746/jkfn.2013.42.10.1707.

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44

Lejczak, B., P. Kafarski, and E. Makowiecka. "Phosphonic analogues of tyrosine and 3,4-dihydroxyphenylalanine (dopa) influence mushroom tyrosinase activity." Biochemical Journal 242, no. 1 (1987): 81–88. http://dx.doi.org/10.1042/bj2420081.

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A series of phosphonic analogues of tyrosine and 3,4-dihydroxyphenylalanine (dopa) were synthesized in order to study their interaction with mushroom tyrosinase. 1-Amino-2-(3,4-dihydroxyphenyl)ethylphosphonic acid and 1-amino-2-(3,4-dimethoxyphenyl)ethylphosphonic acid turned out to be substrates for mushroom tyrosinase with Km values of 3.3 mM and 9.3 mM respectively. Shortening of the alkyl chain by one methylene group gave amino-(3,4-dihydroxyphenyl)methylphosphonic acid, one of the most powerful known inhibitors of this enzyme. This compound, racemic as well as in its optically active form

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Batubara, Irmanida, Yuni Kartika, and Latifah K. Darusman. "Relationship between Zingiberaceae Leaves Compounds and its Tyrosinase Activity." Biosaintifika: Journal of Biology & Biology Education 8, no. 3 (2016): 371. http://dx.doi.org/10.15294/biosaintifika.v8i3.6742.

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<p>The leaves of Zingiberaceae family has not been much explored its potential, especially as a skin whitener. The relationship between total anthocyanins, chlorophyll, carotenoids and tannins contents of <em>Zingiberaceae </em>leaves and tyrosinase activity were determined. Ten species of <em>Zingiberaceae </em>were separated by <em>n</em>-hexane and the residues were extracted with ethyl acetate. The total anthocyanins, chlorophyll, carotenoids, tannins contents and the activities of ethyl acetate extracts were determined by spectrometric method. The

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Athipornchai, Anan, Nattisa Niyomtham, Wachirachai Pabuprapap, et al. "Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies." Cosmetics 8, no. 2 (2021): 35. http://dx.doi.org/10.3390/cosmetics8020035.

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Natural tyrosinase inhibitors from herbal plants are promising therapeutic agents for skincare and cosmetic products. Natural curcuminoids exhibit weak antityrosinase properties. The structural modification of curcumin, the major curcuminoid from Curcuma longa, gave 14 analogues. The tyrosinase inhibitory activity of the natural curcuminoids and the modified analogues on both L-tyrosine and DOPA substrates were evaluated. The inhibition kinetics were also undertaken. For analogues with potent activity on the L-tyrosine substrate, the isoxazole analogue 12 and two reduced analogues, hexahydrocu

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Jiang, Chao, Ya Li, Chenghui Liu, Liying Qiu, and Zhengping Li. "A general and versatile fluorescence turn-on assay for detecting the activity of protein tyrosine kinases based on phosphorylation-inhibited tyrosyl oxidation." Chemical Communications 52, no. 85 (2016): 12570–73. http://dx.doi.org/10.1039/c6cc07035c.

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Arifianti, Ayun Erwina, Effionora Anwar, and Nurjanah Nurjanah. "Tyrosinase Inhibitor and Antioxidant Activity of Seaweed Powder from Fresh and Dried Sargassum plagyophyllum." Jurnal Pengolahan Hasil Perikanan Indonesia 20, no. 3 (2018): 488. http://dx.doi.org/10.17844/jphpi.v20i3.19769.

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<p>Sargassum plagyophyllum from Sargassaceae family contains various bioactive compounds, namely<br />phlorotannin which is reported as an antioxidant and tyrosinase inhibitor. Tyrosinase inhibitor and<br />antioxidant activity from seaweed powder that obtained from seaweed’s slurry have not been reported. Thus,<br />this study was aimed to obtain the best seaweed slurry and powder from S. plagyophyllum based on tyrosinase<br />inhibitor and antioxidant activity, so it can be used as active substance in skin lightening cosmetic formula.<br />S. plagyophyllum

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Frederick O.Ujah, Paschal H. Nenge, Roseline T. Kassar, Abugh, S. Hough, and Alvin I. Aondona. "Isolation, partial purification and immobilization of locally sourced tyrosinase on different fiber materials." Open Access Research Journal of Science and Technology 1, no. 1 (2021): 042–50. http://dx.doi.org/10.53022/oarjst.2021.1.1.0025.

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Tyrosinase has diverse functions in biological systems including melanin synthesis for defense against harmful effects of ultraviolet light. It oxidizes tyrosine especiallyL-3, 4-dihydroxyphenylalanineto L-Dopaquinone. The objective is to isolate, partially purify and immobilize tyrosinase on coconut fiber and palm wood chips using gum Arabic as binder. Yam (Dioscorea rotundata) was used as source of tyrosinase. It was extracted by mashing yam with potassium phosphate buffer (PH 7). The slurry was centrifuged, supernatant decanted and mixed with solid ammonium sulphate [(NH4)2SO4] for partial

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50

Im, Do-Youn, and Kyoung-In Lee. "Antioxidative and Antibacterial Activity and Tyrosinase Inhibitory Activity of the Extract and Fractions from Taraxacum coreanum Nakai." Korean Journal of Medicinal Crop Science 19, no. 4 (2011): 238–45. http://dx.doi.org/10.7783/kjmcs.2011.19.4.238.

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