Antityrosinase and antimicrobial activities of 2-phenylethanol, 2-phenylacetaldehyde and 2-phenylacetic acid

Zhu, Yujing; Zhou, Hantao; Hu, Yonghua; Tang, Jian-Yang; Su, Mingxing; Guo, Yun-Ji; Chen, Qing‐Xi; Liu, Bo

doi:10.1016/j.foodchem.2010.06.036

Cited by 119 publications

(73 citation statements)

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“…Seo et al 8 reviewed the importance of mushroom tyrosinase and defines its biochemical character and inhibition and activation by several inhibitors from natural and synthetic origin. Zhu et al 9 also reported that tyrosinase enzyme has also been linked to Parkinson's disease. Loizzo et al 10 and Chang 11 reviewed the tyrosinase inhibitors from both natural and synthetic origin for their use in food and cosmetic industry.…”

Section: Introductionmentioning

confidence: 99%

Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors

Ashraf

Rafiq

Seo

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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A series of umbelliferone analogues were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that some of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. Especially, 2-oxo-2-[(2-oxo-2H-chromen-7-yl)oxy]ethyl-2,4-dihydroxybenzoate (4e) bearing 2,4-dihydroxy substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with IC 50 value 8.96 mM and IC 50 value of kojic acid is 16.69. The inhibition mechanism analyzed by LineweaverBurk plots revealed that the type of inhibition of compound 4e on tyrosinase was noncompetitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that compounds 4c and 4e may serve as a structural template for the design and development of novel tyrosinase inhibitors.

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Section: Introductionmentioning

confidence: 99%

Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors

Ashraf

Rafiq

Seo

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…According to ZHU et al (2011) it occurs naturally in essential oils of flowers as hyacinth, jasmine, lilies and daffodils, however, concentrations are too low to justify extraction (SENDOVSKI et al, 2010), with the exception of rose oil that contains up to 60% PE. High percentages of FE can be obtained by steam drag distillation and solvent extraction.…”

Section: Introductionmentioning

confidence: 99%

Production of natural aroma by yeast in wastewater of cassava starch industry

et al. 2015

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2-Phenylethanol (PE) is an aromatic alcohol with a characteristic odor of roses, widely used in food industry to modify certain aroma compositions in formulations with fruit, jam, pudding, and chewing gums, and also in cosmetic and fragrance industry. This compound occurs naturally in low concentrations in some essential oils from flowers and plants. An alternative to plants extraction are biotechnological processes. This study evaluated 2-phenylethanol's production in cultivation of Saccharomyces cerevisiae in cassava wastewater originated from starch industry. The substrate was supplemented with glucose and L-phenylalanine in order to obtain higher 2-phenylethanol concentrations and better efficiency in glucose/2-phenylethanol conversion. It was performed using Rotatable Center Composite Design and response surface analysis. Cultures were performed under aerobic conditions in a batch system in Erlenmeyer flasks containing 50 mL of medium in shaker at 150 rpm and 24 ± 1 ºC. The highest PE values were obtained with supplementation of 20.0 g.L -1 of glucose and 5.5 g.L -1 of L-phenylalanine, which has been experimentally validated, obtaining a PE production of 1.33 g.L -1 and PE/glucose yield factor of 0.070 g.g -1 , equivalent to 74.3 and 89.7% of desirability values according to the validated model.

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Section: Introductionmentioning

confidence: 99%

“…There are many tyrosinase inhibitors, such as hydroquinone (Garcia and Fulton Jr, 1996), ascorbic acid (Kameyama et al, 1996), arbutin (Nakajima et al, 1998), kojic acid (Mishima et al, 1994), aromatic aldehydes (Jimenez et al, 2001;, aromatic acids (Chen et al, 2005;Si et al, 2011), aromatic alcohol (Liu et al, 2007;Zhu et al, 2011), and tropolone (Valero et al, 1991). It has been suggested that the addition of a methoxy group at the meta or para position of salicylaldehyde shows different inhibition strength.…”

Section: Introductionmentioning

confidence: 99%

“…Alkoxybenzoic acids have been studied for the inhibition of mushroom tyrosinase (Huang et al, 2006), revealing that different alkoxy substitutions induce various inhibition type (Chen et al, 2005). The inhibition of 2′-phenylethanol, 2′-phenylacetaldehyde and 2′-phenylacetic acid on the activity of mushroom tyrosinase indicating that the functional group on the benzene ring group played an important role in the enzyme inhibition (Zhu et al, 2011).Paeonol (structure was shown in Fig. 1(a)), belonging to aromatic ketone, one of the primary bioactive components concentrations of effector (dissolved in DMSO solution), was added to 2.8 mL L-DOPA in Na 2 HPO 4 -NaH 2 PO 4 buffer (50 mM, pH 6.8), and then 0.1 mL of aqueous solution of mushroom tyrosinase was added to the assay mixture with a total volume of 3 mL.…”

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confidence: 99%

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Tyrosinase Inhibitory Effects and Antioxidant Properties of Paeonol and Its Analogues

Zhu

Cao

2013

FSTR

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With the aim to find out structural features for the tyrosinase inhibitory activity, the inhibitory effects of seven paeonol analogues on the diphenolase of mushroom tyrosinase, the interaction between the inhibitors and the copper ions, and the antioxidant activity by DPPH radical were investigated. These paeonol analogues had suggested remarkable inhibition toward tyrosinase. Among them, paeonol (a) exhibited the strongest inhibition activity (IC 50 =0.21 mM) as well as showed potent scavenging activity on the DPPH radical. The inhibition kinetics revealed that paeonol (a) was a mixed-type inhibitor, 2′-hydroxy acetophenone (c), 4′-hydroxy acetophenone (d), and 2,4′-dihydroxy acetophenone (e) were competitive inhibitors, while acetophenone (b), 2′-methoxyacetophenone (f), and 4′-methoxy acetophenone (g) behaved as noncompetitive inhibitors. The maximum absorbing wavelengths of compounds (c), (d), and (e) showed different significant blue shifts, which could explain that they exhibited competitive inhibition by forming a chelate with the copper ions at the catalytic domain of the tyrosinase.Keywords: paeonol, acetophenone, tyrosinase inhibitor, DPPH radical, copper ions chelation *To whom correspondence should be addressed. E-mail: yuyanying@ncu.edu.cn IntroductionTyrosinase (EC 1.14.18.1), known as polyphenol oxidase, is a multifunctional copper-containing metalloenzyme widely distributed in nature. It mainly catalyzes the o-hydroxylation of monophenols to the corresponding catechols, and the oxidation of monophenols to the corresponding o-quinones (Yoon et al., 2009). Consequently, a series of high reactive quinones are produced to initiate the pigmentation and excessive activation of tyrosinase can cause various dermatological disorders, such as Parkinson and other degenerative diseases (Asanuma et al., 2003).One of the reactions catalyzed by the tyrosinase is the oxidation of L-dopa to L-dopaquinone by utilising molecular oxygen. In addition, reactive oxygen species (ROS) and free radical-mediated reactions are associated with various diseases, such as diabetes mellitus, cancer, ageing, skin disorders, and neurodegenerative diseases (Pham-Huy et al., 2008). If the inhibitors we have designed can weaken the tyrosinase activity as well as scavenge ROS effectively, the production of melanin and the damage of ROS to our human beings will be decreased to a great extent. Hence, tyrosinase inhibitors have become increasingly important in cosmetic (Guevara and Pandya, 2001) and medicinal (Kanost et al., 2004) industry, the food industry (Lunadei et al., 2011) and agriculture (Guerrero and Rosell, 2005) to prevent hyperpigmentation.In recent years, a large number of naturally occurring and synthetic tyrosinase inhibitors have been reported. There are many tyrosinase inhibitors, such as hydroquinone (Garcia and Fulton Jr, 1996), ascorbic acid (Kameyama et al., 1996), arbutin (Nakajima et al., 1998), kojic acid (Mishima et al., 1994, aromatic aldehydes (Jimenez et al., 2001;, aromatic acids (Chen et al., 2005;Si et a...

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Antityrosinase and antimicrobial activities of 2-phenylethanol, 2-phenylacetaldehyde and 2-phenylacetic acid

Cited by 119 publications

References 24 publications

Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors

Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors

Production of natural aroma by yeast in wastewater of cassava starch industry

Tyrosinase Inhibitory Effects and Antioxidant Properties of Paeonol and Its Analogues

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