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Genesys 10 s uv vis spectrometer

Manufactured by Thermo Fisher Scientific
Sourced in United States

The Genesys 10 S UV-Vis Spectrometer is a laboratory instrument designed for ultraviolet and visible light spectroscopy. It is capable of analyzing the absorption or transmittance of light by samples in this wavelength range.

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21 protocols using genesys 10 s uv vis spectrometer

1

Antioxidant Activity of Soursop Fruit Tea

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The antioxidant activity was evaluated in vitro by DPPH scavenging method. A total of 1 g of soursop fruit tea was weighed, homogenized with 50 mL of ethanol, and filtered to obtain the extract. The extract (0.5 mL) was placed in a test tube and added with 1.5 mL of DPPH. The sample was incubated in darkness for 30 min before optical absorbance measurement using Thermo Scientific GENESYS 10S UV–Vis Spectrometer at a wavelength of 517 nm (Brand‐Williams et al., 1995 (link); Tran et al., 2023 (link)).
The antioxidant activity was evaluated in vitro by the ABTS scavenging method as previously described by Nguyen et al. (2023 (link)). A total of 1 g of soursop fruit tea was weighed, homogenized with 50 mL of ethanol, and filtered to obtain the extract. The extract (0.5 mL) was mixed with 1.5 mL of ABTS in a test tube. The sample was incubated in the dark for 30 min before measurement by using Thermo Scientific™ GENESYS 10S UV–Vis Spectrometer at a wavelength of 734 nm.
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2

Spectrophotometric Determination of Soursop Fruit Tea Polyphenols

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Total polyphenol content of soursop fruit tea extract was determined by the Folin–Ciocalteu colorimetric method, using gallic acid as a standard and previously described by Gyesi et al. (2019 (link)) and Dao et al. (2021 (link)). A total of 1 g of soursop fruit tea was weighed, homogenized with 50 mL of ethanol, and filtered to obtain the extract. The extract (0.1 mL) was placed in a dark‐colored test tube and added with 0.5 mL of FCR 10%, and 0.4 mL 7.5% Na2SO3. The sample was incubated in the dark for 1 h before absorbance measurement at the wavelength of 765 nm using GENESYS™ 10S UV–Vis spectrometer (Thermo Scientific, USA). TPC is expressed in milligrams of Gallic acid equivalent (GAE) and calculated by Equation (5). TPC=Cx×n×V×100m×100X×103, where Cx is the concentration of gallic acid determined from the standard curve (μg/mL): Cx=61.0676×A+1.8598, R = 0.9991; n is the dilution from the original extract; V is the volume of the original extract (mL); X is the sample moisture (%) and m is the weight of sample (g).
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3

Enzyme Encapsulation Efficiency Determination

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The obtained supernatants were carefully removed from the precipitated NPs, then diluted to a suitable range with purified water and the absorption was measured by using a UV spectrometer (ThermoScientific-Genesys 10 S UV-Vis Spectrometer, USA) at lambda max 281 nm. Based on the absorbance, the concentration of unprecipitated NP enzymes was used to calculate precipitation efficiency.
The obtained supernatants were carefully separated from the encapsulated NPs and absorption was measured at 281 nm for each sample based on a pre-recorded calibration line. The concentration of free enzyme NPs was measured for all samples, from which encapsulation efficiency was determined. Encapsulation efficiency (EE%) resulting from the adsorption of alginate on the LYS composite was calculated according to the following equation:
EE%=(totalamountofLYS(mg)amountofLYZinthesupernatantsol.(mg))totalamountofLYS(mg)*100
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4

Cytochrome C Reduction Assay with Anatase NPs

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Cytochrome C (Cyt-C) reduction assay was carried out in a 24 well plate, each well containing 2 ml of oxidized Cyt C solution (0.1 mM of Cyt-C in PBS buffer, pH 7.4) and 0–0.8 mg of anatase NPs (A-NPs), stirred with a micro magnetic bar. The wells were exposed to a light source for up to 30 minutes. Dark conditions in the control wells were obtained by covering the wells with aluminum foil. One ml samples were withdrawn and the A-NPs were sedimented by centrifugation (Heraeus, Thermo Fisher Scientific, Waltham, MA) at 17 800g for 15 minutes. Optical densities of the supernatants (0.5 ml) were examined at 450 and 550 nm by a Genesys 10S UV-VIS spectrometer (Thermo Fisher, Waltham, MA, USA) to follow Fe3+Cyt-C reduction to Fe2+Cyt C, 1 mM reduced Cyt C = 23.65 OD 550 nm.33 (link)
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5

Materials Characterization Using Advanced Techniques

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The SEM images were observed using a JEOL JSM-5600LV (Akishima, Tokyo). Infrared data were measured using a VERTEX 70-FT IR spectrometer (Billerica, MA, USA). A total of 16 scans were signal-averaged with a resolution of 8 cm−1. The analysis was performed using thermogravimetric analysis (TGA Q50M, TA instruments, New Castle, DE, USA) to measure the thermal strength. UV was measured using a Genesys 10S UV–Vis spectrometer (ThermoFischer, Waltham, MA, USA).
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6

Enzyme Activity Determination of LYS in SEDDS

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After incorporation of LYS:SDS complex in liquid SEDDS preconcentrate, 100 µL of preconcentrate was emulsified in 1 mL of phosphate buffer, 6.8 pH at 37 °C, and 300 rpm (1:10 dilution). Liquid SEDDS loaded with LYS:SDS complex was adsorbed onto a solid carrier (1:2 ratio), and 100 mg of the prepared solid SEDDS was also emulsified in 1 mL of phosphate buffer, 6.8 pH at 37 °C, and 300 rpm (1:10 dilution). Then, 100 µL of each resulting emulsion was added to 2.5 mL of 0.25 mg/mL bacterial suspension of M. lysodeikticus and mixed with inversions for 20 s in a quartz cuvette. The activity of LYS was determined by measuring the degradation of a bacterial suspension at 450 nm every 5 s using a UV spectrometer (Genesys 10 S UV-VIS Spectrometer, Thermo Fisher Scientific Inc., Waltham, MA, USA). Enzyme activity (%) of LYS in SEDDS was compared to the activity of corresponding LYS:SDS complex as well as freshly prepared free LYS solution.
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7

Comprehensive Nanomaterial Characterization Techniques

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Nicolet 710 FT-IR spectrometer (Thermo Nicolet, USA) was employed to analyze the FTIR results. The metal content was determined by IRIS Advantage OPTIMA 7000DV Inductively Coupled Plasma-Atomic Emission Spectrometer (Thermo PerkinElmer). The surface morphology observation, particle size measurement analysis, and scanning electron microscope images of the NPs were determined by SUPRA™ 55 Thermal Field Emission Scanning Electron Microscopy (Carl Zeiss, Germany). The transmission electron microscope images of NPs were studied by JEM-2100F Transmission Electron Microscopy (JEOL, Japan). X-ray diffraction studies were carried out on EMPYREAN X-ray diffractometer (PANalytical, Netherlands). Genesys 10S UV-Vis spectrometer (Thermo Fisher) was used for the ultra-violet and visible spectral analysis. For XPS analysis, Escalab 250xi X-ray photoelectron spectroscopy (Thermo, USA), and for DLS and Zeta potential analysis, NanoBrook Omni (Brookhaven Instruments, USA) were used.
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8

Chlorophyll Content and Fluorescence Analysis

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Absorption spectra were recorded at room temperature using Genesys 10 S UV-Vis spectrometer (Thermo Scientific) and VisionLite software version 4.0. The spectra were recorded from 350 to 750 nm in 1 nm intervals. Chlorophyll content was determined by measuring the absorbance at 645 nm and 663 nm and calculated according to Porra et al.24 (link). Fluorescence analysis of reconstituted LHCBM6 in sucrose buffer and of TiO2/ITO plates with and without proteins were performed with Tecan infinite M200 Reader in 96-well plates and 6-well plates, respectively. Spectra were measured with excitation wavelength 440 nm, 475 nm and 500 nm. Emission was recorded from 600 nm to 800 nm in 2 nm intervals.
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9

Analytical Characterization of Compounds

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Optical rotations were measured with an Anton Paar MCP 200 polarimeter with a sodium lamp (589 nm) (Anton Paar GmbH, Graz, Austria). UV spectra were obtained on Genesys 10S UV-Vis spectrometer (Thermo Fisher Scientific Ltd, Waltham, MA, USA); IR spectra were recorded with a Nicolet IS5 FT-IR spectrometer (Thermo Fisher Scientific Ltd, Waltham, MA, USA); NMR spectra were recorded on Bruker AVANCE III 500 spectrometer (Bruker Inc., Karlsruhe, Germany). HPLC-MS were acquired on Agilent 1200HPLC/6520QTOFMS (Agilent Technologies Inc., Santa Clara, CA, USA). Semi-preparative HPLC isolation was performed on Agilent 1260 Infinity II (Agilent Technologies Inc., Santa Clara, USA) with an ODS column (YMC-Triart C18, 10 mm × 250 mm, YMC Co. Ltd., Tokyo, Japan). Silica gel (200–300 and 300–400 mesh) used in column chromatography (CC) and silica gel GF254 (10–40 µm) used in thin layer chromatography (TLC) were supplied by Qingdao Marine Chemical Factory in China.
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10

Enzymatic activity quantification protocol

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For polyphenol oxidase (PPO) activity, the sample (130 μL) was mixed with 300 µL of McIlvaine buffer (0.1 M Na2HPO4) and 170 μL of 0.2 M pyrocatechol solution; then, absorbance was measured for 20 min at 410 nm.
For peroxidase (POD) activity, the sample (100 μL) was mixed with 1000 µL of H2O2 -KPi buffer and 10 μL of 0.04 M o-dianisidine solution in methanol; then, absorbance was measured for 20 min at 460 nm.
The measurements were performed with Genesys 10S UV-Vis Spectrometer (Thermo-Scientific, Waltham, MA, USA), and data were collected with VISIONlite software. Enzyme activity was expressed as U (units) per mg protein. One unit (U) is defined as the change in absorbance in one minute. The protein content was determined with the Bradford method with minor modifications in accordance with Kruger [34 (link)].
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