Enzymic browning of sulphocatechol

When sulphur dioxide inhibits the enzymic browning of catechol catalysed by mushroom tyrosinase, the main reaction product is 4-sulphocatechol. When assessed for its browning potential, this product appears to be unreactive and does not inhibit the enzyme.     

中药降香对酪氨酸酶激活作用的动力学研究

酪氨酸酶是生物合成黑素的主要酶。降香有促进酪氨酸酶活性的作用。通过对中药降香的水提取液和乙醇提取液促进酪氨酸酶活性作用的观察研究及降香提高酪氨酸酶活性的动力学观察研究，得到Lineweaver-Burk曲线、动力学回归方程及米氏常数Km值。为研究中药有效成分激活黑素细胞的机理奠定了基础。     

Application of enzymatically gelled chitosan solutions to water‐resistant adhesives

An investigation was undertaken on the application of dilute chitosan solutions gelled by tyrosinase‐catalyzed reaction with 3,4‐dihydroxyphenethylamine (dopamine). The tyrosinase‐catalyzed reaction with dopamine conferred water‐resistant adhesive properties to the semidilute chitosan solutions. The viscosity of the chitosan solutions increased highly by the tyrosinase‐catalyzed reaction and the subsequent reactions between o‐quinone compounds and chitosan. These highly viscous, gel‐like modified chitosan materials were allowed to spread onto the surfaces of the glass slides, which were tightly lapped together and held them in water. Tensile shear adhesive strength of over 400 kPa was observed for the modified chitosan samples. The increase in the amino group concentration of the chitosan solutions and the molecular mass of the chitosan used effectively led to the increase in adhesive strength of the glass slides. In addition, in the case where the chitosan solution was gelled by the enzymatic reaction with dopamine in the presence of poly(ethylene glycol), adhesive strength sharply increased at shorter reaction times concomitantly with the increase in the viscosity of the chitosan solutions because the tyrosinase activity effectively was retained by poly(ethylene glycol). © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 104: 1818–1827, 2007     

Tyr/MWNTs-Chit/GCE生物传感器的制备及其在快速检测大肠杆菌中的应用

该文基于多壁碳纳米管(muhiwalled carbon nanotubes,MWNTs)-壳聚糖(Chit)复合物修饰电极制备了灵敏、稳定的酪氨酸酶(tyrosinase.Tyr)生物传感器.由于MWNTs-Chit复合物具有好的生物兼容性以及电催化能力,Tyrr/MWNTs-Chit/GCE生物传感器在苯酚的检测中具有高灵敏度(412 mA/mo1),低检测限(5.0nmol/L),较宽的线性范围(1.0×10-8～2.8×10-5mol/L)以及良好的稳定性(10天后仍保持93%的活性).把Tyr/MWNTs-Chit/GCE生物传感器进一步应用于大肠杆菌的检测,大肠杆菌在104～107 cfu/mL范围内与电流响应成正比;经过5.0 h的培养,进一步降低大肠杆菌的检测限至10 cfu/mL.     

Enzymatic Writing to Soft Films: Potential to Filter,Store, and Analyze Biologically Relevant Chemical Information

Sensor‐based chemical analyses commonly enlist either the molecular recognition capabilities of biology (e.g., enzyme biosensors) or advanced information processing algorithms (e.g., the electronic nose). Here, a hybrid approach is proposed in which an enzyme is used to “filter” chemical information and write this information to a film which then serves as a permanent storage medium that can be ‘read’ repeatedly, interactively, and by multiple sensor modalities. This approach is demonstrated by analyzing common dietary phenols that are reported to offer health benefits. Specifically, the enzyme tyrosinase is used to convert these phenols into reactive quinones that graft (i.e., write) to a chitosan film. Grafting can be detected by optical, mechanical, and electrochemical sensors. Importantly, grafting confers redox activity to the films and this redox activity can be probed interactively by advanced electrochemical methods that allow the intrinsic redox reactivities to be compared, redox interactions to be identified, and biologically relevant redox activities to be examined. The transfer of chemical and biological information to a film is envisioned to provide broader access to the extensive capabilities offered by sensor technologies and signal processing methodologies.     

Dual Bioactivities of Essential Oil Extracted from the Leaves of Artemisia argyi as an Antimelanogenic versus Antioxidant Agent and Chemical Composition Analysis by GC/MS

The study was aimed at investigating the antimelanogenic and antioxidant properties of essential oil when extracted from the leaves of Artemisia argyi, then analyzing the chemical composition of the essential oil. The inhibitory effect of the essential oil on melanogenesis was evaluated by a mushroom tyrosinase activity assay and B16F10 melanoma cell model. The antioxidant capacity of the essential oil was assayed by spectrophotometric analysis, and the volatile chemical composition of the essential oil was analyzed with gas chromatography-mass spectrometry (GC/MS). The results revealed that the essential oil significantly inhibits mushroom tyrosinase activity (IC₅₀ = 19.16 mg/mL), down-regulates B16F10 intracellular tyrosinase activity and decreases the amount of melanin content in a dose-dependent pattern. Furthermore, the essential oil significantly scavenged 2,2-diphenyl-1-picryl-hydrazyl (DPPH) and 2,2′-azino-bis (3-ethylbenzthiazoline- 6-sulphonic acid) ABTS radicals, showed an apparent reduction power as compared with metal-ion chelating activities. The chemicals constituents in the essential oil are ether (23.66%), alcohols (16.72%), sesquiterpenes (15.21%), esters (11.78%), monoterpenes (11.63%), ketones (6.09%), aromatic compounds (5.01%), and account for a 90.10% analysis of its chemical composition. It is predicted that eucalyptol and the other constituents, except for alcohols, in the essential oil may contribute to its antioxidant activities. The results indicated that essential oil extracted from A. argyi leaves decreased melanin production in B16F10 cells and showed potent antioxidant activity. The essential oil can thereby be applied as an inhibitor of melanogenesis and could also act as a natural antioxidant in skin care products.     

An evaluation of extracts of five traditional medicinal plants from Iran on the inhibition of mushroom tyrosinase activity and scavenging of free radicals

This study aimed to evaluate the free radical scavenging and inhibition properties of five medicinal plants, including Quercus infectoria Olive., Terminalia chebula Retz. , Lavendula stoechas L., Mentha longifolia L., Rheum palmatum L., toward the activity of mushroom tyrosinase using l -tyrosine and l -3,4-dihydroxyphenylalanine ( l -DOPA) as the substrate. The methanol extracts of Q. infectoria and T. chebula showed strong radical scavenging effect in 2,2'-dipheny l -1-picrylhydrazyl (DPPH) assay (IC₅₀ = 15.3 and 82.2 μg mL⁻¹ respectively). These plants also showed inhibitory effects against the activity of mushroom tyrosinase in hydroxylation of l -tyrosine (85.9% and 82.2% inhibition, respectively). These two plants also inhibited the oxidation of l -DOPA similar to kojic acid as positive control (IC₅₀ = 102.8 and 192.6 μg mL⁻¹ respectively). In general Q. infectoria and T. chebula significantly inhibited tyrosinase activity and DPPH radical. Both activities were concentration-dependant but not in linear manner. It is needed to study the cytotoxicity of these plant extracts in pigment cell culture before further evaluation and moving to in vivo conditions.     

Repositioning of Thiourea-Containing Drugs as Tyrosinase Inhibitors

Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: The hydroxylation of tyrosine to dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to dopaquinone. Developing functional modulators of tyrosinase is important for therapeutic and cosmetic purposes. Given the abundance of thiourea moiety in known tyrosinase inhibitors, we studied other thiourea-containing drugs as potential tyrosinase inhibitors. The thiourea-containing drugs in clinical use were retrieved and tested for their ability to inhibit tyrosinase. We observed that methimazole, thiouracil, methylthiouracil, propylthiouracil, ambazone, and thioacetazone inhibited mushroom tyrosinase. Except for methimazole, there was limited information regarding the activity of other drugs against tyrosinase. Both thioacetazone and ambazone significantly inhibited tyrosinase, with IC₅₀ of 14 and 15 μM, respectively. Ambazone decreased melanin content without causing cellular toxicity at 20 μM in B16F10 cells. The activity of ambazone was stronger than that of kojic acid both in enzyme and melanin content assays. Kinetics of enzyme inhibition assigned the thiourea-containg drugs as non-competitive inhibitors. The complex models by docking simulation suggested that the intermolecular hydrogen bond via the nitrogen of thiourea and the contacts via thione were equally important for interacting with tyrosinase. These data were consistent with the results of enzyme assays with the analogues of thiourea.