Some enzymes were used: laccase (EC 1.10.3.2) from Pleurotus pulmonarius (also formerly known as P. sajor-caju [51 (link)]), horseradish peroxidase (HRP, EC 1.11.1.7, Sigma-Aldrich, Milan, Italy) from Armoracia rusticana, lignin peroxidase (LiP, EC 1.11.1.14, Sigma-Aldrich) from Phanerochaete chrysosporium, and manganese peroxidase (MnP, EC 1.11.1.13, Sigma-Aldrich) from Ph. chrysosporium. When these enzymes were used, the composition of assay mixtures were changed where appropriate with the systematic omission of the biomimetic catalyst as follows: laccase, 23 E.U., 50 mM potassium phosphate buffer (pH 6); HRP, 3 E.U., 50 mM potassium phosphate buffer (pH 7), 8.8 mM H2O2; LiP, 0.05 E.U., 50 mM sodium citrate buffer (pH 3), 0.176 mM H2O2; MnP, 0.02 E.U., 50 mM sodium citrate buffer (pH 3), 0.176 mM H2O2, 2mM Mn(II) acetate, dissolved in 50 mM sodium malonate buffer (pH 4.5).
Laccase
Manufactured by Merck Group
Sourced in United States
Laccase is an oxidoreductase enzyme that catalyzes the oxidation of various aromatic and non-aromatic compounds, including phenols, polyphenols, diamines, and lignin. It is primarily used in industrial and research applications.
Automatically generated - may contain errors
Lab products found in correlation
Glutaraldehyde, by Merck Group (4 mentions)
2 2 azino bis, by Merck Group (3 mentions)
Glucose oxidase, by Merck Group (3 mentions)
Trametes versicolor, by Merck Group (3 mentions)
Trypsin edta, by Thermo Fisher Scientific (3 mentions)
D glucose, by Merck Group (2 mentions)
Diammonium salt, by Merck Group (2 mentions)
Chitosan, by Merck Group (2 mentions)
Syringaldehyde, by Merck Group (2 mentions)
Nafion, by Merck Group (2 mentions)
Tyrosinase, by Merck Group (2 mentions)
Fetal bovine serum (fbs), by Thermo Fisher Scientific (2 mentions)
Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (2 mentions)
Lignin peroxidase, by Merck Group (1 mentions)
Horseradish peroxidase, by Merck Group (1 mentions)
Indium tin oxide, by Merck Group (1 mentions)
Sodium perchlorate, by Merck Group (1 mentions)
L ascorbic acid, by Thermo Fisher Scientific (1 mentions)
Uric acid, by Thermo Fisher Scientific (1 mentions)
Glucose oxidase gox, by Merck Group (1 mentions)
45 protocols using laccase
1
Enzyme-Catalyzed Oxidative Reactions
2
Curdlan Hydrogel Enzyme Immobilization
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Immobilization of laccase and peroxidase on uncoated and polycatecholamine-coated curdlan hydrogels was performed by incubation of lyophilized slices (ø 13 mm. 3 mm) in 0.5 mg/mL laccase or peroxidase (Sigma-Aldrich, USA) in Britton-Robinson buffer pH 8.5, in proportion 33.3 mL of enzyme solution/1 g lyophilized curdlan hydrogel slices. The process included 12 h of shaking at 25 °C (DTS-4 shaker, 100 rpm), followed by 36 h incubation at 4 °C for laccase and 24 h incubation at 4 °C for peroxidase. Then, slices were washed in 10 mL DI water, frozen at −20 °C and lyophilized.
The amount of immobilized enzyme was measured quantitatively from the difference between protein concentration in laccase or the peroxidase solution before and after incubation with curdlan hydrogels. Protein concentration was estimated according to Schacterle-Pollack method [56 ]. The results were presented in µg protein/g of dry hydrogel weight.
The amount of immobilized enzyme was measured quantitatively from the difference between protein concentration in laccase or the peroxidase solution before and after incubation with curdlan hydrogels. Protein concentration was estimated according to Schacterle-Pollack method [56 ]. The results were presented in µg protein/g of dry hydrogel weight.
3
Electrochemical Biosensor Fabrication
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The following chemicals were purchased from Sigma-Aldrich and were used without further purification: glucose oxidase (GOx) from Aspergillus niger (128.2 U∙mg−1 solid), laccase from Trametes versicolor (12.9 U∙mg−1 solid), N-hydroxysulfosuccinimide (NHS; 98%), N-ethyl-N’(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC; 98%), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), multi-walled carbon nanotubes (MWCNTs; carboxylic acid-functionalized), sodium perchlorate (NaClO4, 98%), D-(+)-glucose, ferrocenemethanol (FcCH2OH), and indium tin oxide (ITO) glass (15 Ω.sq−1). Uric acid (99%), L-(+)-ascorbic acid (99+%), and 4-acetamidophenol (98%) were purchased from Alfa Aesar, South Korea. The aqueous solutions were prepared in deionized (DI) water. Polydimethylsiloxane (PDMS; Sylgard 184, Dow Corning, Midland, MI, USA) was mixed in a 10:1 ratio of base and curing agent. All analytical experiments were performed in a sodium phosphate buffer prepared with 50 mM NaH2PO4 and 50 mM Na2HPO4; the pH was adjusted by their proper mixing.
4
Laccase-Mediated Degradation of Sulfamethoxazole
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Halloysite nanoclay (diameter × length- 30–70 nm × 1–3 μm, nanotube), sulfamethoxazole (SMX, analytical standard), laccase from Trametes versicolor (form- powder), sodium sulfite (Na2SO3, ACS reagent grade), sodium hydroxide (NaOH, ACS reagent grade), 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS, assay- ≥98% high-performance liquid chromatography (HPLC)), syringaldehyde (SA, assay- ≥98%), guaiacol (GUA, assay- ≥98%), methanol (HPLC grade), glutaraldehyde (GTA, grade II, 25% in H2O), and chitosan (75–85% deacetylated, low molecular weight, molecular weight- 50,000–190,000 Da) were obtained from Sigma-Aldrich (St. Louis, MO, USA). FeCl3-6H2O was obtained from JUNSEI (Kyoto) Japan. laccase from Trametes versicolor have a molecular mass of 70 kDa and an isoelectric point (pI) of 3.5 [23 (link)].
5
Laccase-Nafion-ABTS Enzyme System
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Laccase, Nafion and 2,2’-azinobis(3-ethylbenzothiazole-6-sulfonic acid) (ABTS) were purchased from Sigma-Aldrich. Other chemical reagents were obtained from Sinopharm Group Chemical Reagent Co., Ltd. (Shanghai, China). All reagents were analytical grade and used without further purification. All aqueous solutions were prepared with Milli-Q purified water (>18.0 MΩ·cm). The acetate buffer system (containing 0.2 M HAC-NaAC) was selected as buffer solution.
6
Laccase-Catalyzed Luciferin Synthesis
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The participation of laccase in luciferin enzymatic synthesis was assayed using commercial laccase from Rhus vernicifera (Sigma, USA) in the presence of hydroquinone (HQ) or dopamine (DA), and d -cysteine. The reactions were initially performed by mixing 10 μL of laccase (0.5 U) and 25 μL of 40 mM HQ or DA, in a final volume of 100 μL of 0.10 M phosphate buffer at pH 6.5, or 90 mM Tris–HCl buffer pH 7.5 in the Elisa plate wells followed by incubation during 1 h at 22 °C under moderate agitation. After that, 12.5 μL of 80 mM d -cysteine were added to the wells with further incubation during 18 h. The control reactions were performed in the absence of d -cysteine or laccase. Luciferin synthesis in each reaction was luminometrically evaluated by bioluminescence in the presence of Amy luciferase and ATP. This assay was carried out by mixing 25 μL of the reaction product, 5 μL of Amy luciferase (~ 3 µg), 5 μL of solution containing 80 mM MgSO4/40 mM ATP, and 65 μL of 0.10 M Tris–HCl buffer at pH 8.0. The reactions were performed in triplicate, and the bioluminescent activities were normalized in relation to the activity of the control reaction between hydroquinone and cysteine at pH 7.5. In order to check luciferin formation, we also carried out TLC of these samples, as described in the topic 2.3.
7
Enzymatic Synthesis of Cellobionic Acid
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Synthesized cellobionic acid was made by enzymatic conversion of 50 g/L cellobiose using 1 U/mL cellobiose dehydrogenase (CDH) (purified from Pichia pastoris [39 (link)]) 1 U/mL laccase from Pleurotus ostreatus (Sigma Aldrich (Saint Louis, MO)), 0.5 mM 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid (ABTS), and 30 mM sodium citrate mixed together to a total volume of 5 mL in a 125 mL baffled flask. This solution was kept at 30°C, 250 rpm for 24 hours. Complete conversion of cellobiose to CBA was confirmed with LC-MS (UC Davis Mass Spec facility) [17 (link)].
8
Fungal Enzyme-Catalyzed Terpene Biotransformation
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Homogenized fungal suspensions were grown in 500mL of medium (SSC) in 1-L Erlenmeyer flasks. After 7 days, the mycelia were removed by filtration using Whatman No. 42 filter papers. The filtrates (50 mL) were transferred to 250-mL flasks containing 25 mg of substrate, and then placed in a stationary incubator at 26℃. Two enzymes, laccase (Sigma-Aldrich) purified from Trametes versicolor and peroxidase (Sigma-Aldrich) from horseradish, were purchased from Sigma-Aldrich. Experiment was performed in 10 mL reaction tube with 0.1M sodium tartarate buffer solution at pH 4.5. laccase and horseradish peroxidase were added to make a final concentration 4U/mL and (-)-α-pinene to a concentration of 0.3mg/mL. Reaction mixture was incubated at room temperature for 6 days.
9
Extraction and Characterization of Arabinoxylan
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AX were obtained from dried distillers’ grains with solubles (DDGS) and characterized as previously described [29 (link)]. The AX presented 64% dry basis (d.b) of pure AX (sum arabinose + xylose), 5.11% glucose, a protein content of 8.2%, an A/X ratio of 1.1 and a molecular weight distribution of 209 kDa. Laccase (benzenediol: oxygen oxidoreductase, E.C.1.10.3.2) from Trametes versicolor, and all other chemical products were purchased from Sigma Chemical Co. (St. Louis, MO, USA).
10
Development of Laccase-PVA-Au Nanofiber Electrode
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Platinum slices with the following dimensions, 10 mm × 10 mm × 1 mm, were polished and cleaned with deionized water ultrasonically to be used as the substrate of the electrode. A batch of 7 wt% PVA solution was prepared as a stock solution by blending 7 g polyvinyl acetate (PVA), Sigma Fw: 14 600–18 600, in 93 ml of reverse osmosis (RO) water at 70 °C. After cooling to room temperature, 10 ml of the PVA stock solution was blended with different weight loading, 2, 4, 6, 8, 10, and 12 mg, of laccase, Sigma Co., and 0.025 g of Au-NPs, Lihochem Co. This blended laccase-PVA-Au-NPs solution was drawn into a syringe for injecting into the electro-spinning equipment, FES-COL Agent Wanted Co., with a flow speed of 0.08 ml min−1. Before spinning, the wettability of the substrate surface was tested with a contact angle meter, Kyowa Face CA-D. The operation voltage and working distance were set to be 18 kV and 15 cm, respectively. After spinning the laccase-PVA-Au-NPs solution on to the substrate, the spun electrode was further sprayed with 5 wt% of H2SO4-contained glutaraldehyde to crosslink the PVA linkage for 15 min. The cross-linked electrode was subjected to a series of microstructural investigations, including SEM (3000 H Hitachi Co.), energy dispersive spectroscopy (Noran Voyager 2.0) and phase identification (D8-SSS Bruker Co.).
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