The activities of soil invertase, urease, and alkaline phosphatase were determined by quantifying the release of glucose, NH3–N, and P2O5 products in soil samples. Soil solutions of 8% sucrose, 10% urea, and 0.5% disodium phenyl phosphate were used as the substrate, followed by incubation at 37 °C for 24 h. Absorbance was recorded using spectrophotometry (UV-VIS spectrophotometer, Model UV-2450, Shimadzu, Kiyoto, Japan) at 508, 578, and 660 nm [66 ]. Dehydrogenase activity was evaluated using a colorimetric method based on the determination of triphenyl formazan (TPF) produced after the reduction of 2,3,5-triphenyltetrazolium chloride (TTC) [67 ] spectrophotometrically (UV-VIS spectrophotometer, Model UV-2450, Shimadzu, Kiyoto, Japan) at 485 nm.
Model uv 2450
Manufactured by Shimadzu
Sourced in Japan
The Shimadzu Model UV-2450 is a double-beam UV-Visible spectrophotometer. It is designed to measure the absorbance or transmittance of a sample across a range of ultraviolet and visible light wavelengths.
Automatically generated - may contain errors
Lab products found in correlation
Protein assay kit, by Bio-Rad (1 mentions)
Cn analyzer, by Elementar (1 mentions)
Nutrient broth medium, by Beijing Land Bridge Technology (1 mentions)
Tcc900, by Edinburgh Instruments (1 mentions)
Avaspec hero spectrometer, by Avantes (1 mentions)
Mixed cellulose ester membrane filter, by Advantec (1 mentions)
12 protocols using model uv 2450
1
Soil Enzyme Activity Quantification
2
Biomimetic Coatings Characterization
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The surface morphologies and structures of Samples DF-FL and DF-RL were examined by SEM (XL30, FEI Company Ltd., Hillsboro, OR, USA) and TF-XRD (RINT Ultima X, Rigaku Co., Tokyo, Japan) employing CuKα X-rays.
The coating solutions were clear and induced no spontaneous precipitation during the biomimetic process (24 h immersion of the substrate). Changes in the calcium and phosphorus concentrations and plasmid DNA and fibronectin concentrations of the coating solutions during the biomimetic process were quantified by ICP (Model PS 7800, Hitachi High-Tech Science Co., Tokyo, Japan) and UV-Vis (Model UV-2450; Shimadzu Corporation, Kyoto, Japan), respectively. To determine plasmid DNA concentration, the absorbance was measured at 260 nm. To assess fibronectin concentration, the absorbance was measured at 595 nm using a protein assay kit (Bio-Rad Laboratories, Inc., Hercules, CA, USA) based on the Bradford method. The content of calcium, phosphorus, plasmid DNA, and fibronectin immobilized on the sample surfaces was estimated by subtracting their final concentrations from the initial concentrations in the coating solution. Three substrates were used for each type of sample to obtain a mean value and a standard deviation. The data were compared using Student’s t-test, where the significance level was set at p < 0.05 for each analysis.
The coating solutions were clear and induced no spontaneous precipitation during the biomimetic process (24 h immersion of the substrate). Changes in the calcium and phosphorus concentrations and plasmid DNA and fibronectin concentrations of the coating solutions during the biomimetic process were quantified by ICP (Model PS 7800, Hitachi High-Tech Science Co., Tokyo, Japan) and UV-Vis (Model UV-2450; Shimadzu Corporation, Kyoto, Japan), respectively. To determine plasmid DNA concentration, the absorbance was measured at 260 nm. To assess fibronectin concentration, the absorbance was measured at 595 nm using a protein assay kit (Bio-Rad Laboratories, Inc., Hercules, CA, USA) based on the Bradford method. The content of calcium, phosphorus, plasmid DNA, and fibronectin immobilized on the sample surfaces was estimated by subtracting their final concentrations from the initial concentrations in the coating solution. Three substrates were used for each type of sample to obtain a mean value and a standard deviation. The data were compared using Student’s t-test, where the significance level was set at p < 0.05 for each analysis.
3
Evaluating Fabric Antioxidant Capacity
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The antioxidant activity of the RSB treated fabrics was measured using standard 2, 2-diphenyl-1-picrylhydrazyl (DPPH) free radical entrapment method. DPPH in methanol solution depicts absorption maxima at 517 nm. Untreated and treated fabric samples of the same dimension were placed separately in a known concentration of DPPH solution for 30 min in the dark, and absorbance was measured. The decrease in absorbance of DPPH solution at 517 nm in the presence of fabric is directly proportional to the fabric's antioxidant activity. A UV–visible spectrophotometer (Model UV 2450, Shimadzu) was used to measure the absorbance.
4
Soil Physicochemical Properties Analysis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Soil pH was determined by pH meter using 1:1 water:soil suspension (PHS-3C, LIDA, Shanghai, China). EC (µs cm−1), was measured by microprocessor conductivity meter (DDS-12DW, Xiaoshan, China by taking soil and distilled water (w/v) in a 1:5 ratio. Total nitrogen, organic carbon, and C:N of RGS were measured with a CN Analyzer (Vario Max, Elementar, Germany). Soil organic carbon was measured by the oxidation method with 1N K2Cr2O7 and 98% H2SO4 solution, followed by titration with 0.2 N FeSO4 [62 ]. Total nutrients (N, P, K) of RGS were determined colorimetrically by digesting samples in H2SO4 and HClO4, as described by Reference [63 (link)]. Available phosphorous in soil was determined following Olsen et al. [64 ] in a wet digestion through the calorimetric method of molybdenum antimony resistance, and absorbance was taken at 880 nm using a spectrophotometer (UV-VIS spectrophotometer, Model UV-2450, Shimadzu, Kiyoto, Japan). Available K was extracted using a neutral solution of NH4OAc (1 mol L−1) followed by emission spectroscopy (FP 6410, Shanghai Bante Instrument Co., Ltd., China) [65 ].
5
DPPH Radical Scavenging Activity Assay
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
DPPH radical scavenging activity was determined according to the procedure described by Brand-Williams et al. (1995) with minor modifications. 100 mg of sample was extracted with 1 mL of absolute methanol for 2 h and then centrifuged at 3000 × g for 10 min. The supernatant (100 μL) was collected and reacted with 3.9 mL of a 6 × 10−5 mol/L of DPPH solution. Absorbance (A) (UV–vis spectrophotometer, Model, UV-2450, Shimadzu, Japan) at 515 nm was read at 0 (control) and 30 min (samples) using a methanol blank. Antioxidant activity was measured as % scavenging activity of DPPH radical calculated as below:
6
Isolation and Characterization of Spoilage Bacterium Pseudomonas deceptionensis CM2
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
P. deceptionensis CM2 used in this study was isolated from spoiling chicken meat samples. A single colony of P. deceptionensis CM2 was transferred in 30 mL of nutrient broth (NB) medium (Beijing Land Bridge Technology Co., Ltd., Beijing, China) and incubated under shaking (150 rpm) at 25 °C for 24 h. After centrifugation at 6000× g for 10 min, the cells were collected and washed twice with sterile saline solution. The resulting pellets were resuspended in the same solution and the optical density at 600 nm (OD600) measured with a spectrophotometer (Shimadzu, Model UV 2450). According to the calibration curve for OD600 versus viable cell count, the bacterial solution was diluted to a final concentration of approximately 9 to 10 log10 colony-forming units (CFU)/mL.
7
Protein Concentration in Honey Bee Workers
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
At the end of the study, the wet weight of 20 bees per colony was obtained within 2 h after emergence. Three bees were randomly selected from the 20 bee groups and analyzed for protein concentration. The heads and thoraxes of the three workers were removed and homogenized individually in 1.5-ml Eppendorf microcentrifuge tubes containing a 75-mM phosphate buffer solution (pH 7.4). The samples were centrifuged and analyzed for protein concentration using a PA102 Bradford protein assay kit (Tiangen Biotech Co. Ltd, Beijing, China). Standard curves for estimating protein concentration were prepared using bovine serum albumin. The protein absorbance was measured at 595 nm versus a blank reagent using a Shimadzu spectrophotometer (Model #UV-2450, Shimadzu Corporation, Kyoto, Japan).
8
Measuring Midgut Protease Activity in Bees
Check if the same lab product or an alternative is used in the 5 most similar protocols
The midguts of the 6-d-old bees were excised carefully, placed in Eppendorf tubes containing 100 µl of Tris–HCl (pH 7.9) each, and stored at −80°C for further processing. The total midgut protease activity was measured as described by
Sagili et al. (2005) (link)
. Briefly, frozen guts were crushed using a glass pestle, homogenized in Tris–HCl buffer (pH 7.9), and centrifuged at 10,000 rpm at 4°C for 5 min. The supernatants were used to determine the total midgut proteolytic enzyme activity (
Michaud et al. 1995 (link)
).
Twenty microliters of assay buffer (0.1 M Tris–HCl, pH 7.9) and 60 μl of 2% (w/v) azocasein diluted in assay buffer were added to 5 μl of supernatant. After 6 h of incubation at 37°C, the reaction was stopped by adding 300 μl of 10% (w/v) trichloroacetic acid to each mixture. The tubes were centrifuged for 5 min at 10,000 rpm, and 350 μl of the supernatant was added to 200 μl of 50% ethanol in water. The absorbance of this mixture was measured at 440 nm using a Shimadzu spectrophotometer (Model #UV-2450, Shimadzu Corporation). The total midgut proteolytic activity was expressed as OD
440.
+ Expand
The midguts of the 6-d-old bees were excised carefully, placed in Eppendorf tubes containing 100 µl of Tris–HCl (pH 7.9) each, and stored at −80°C for further processing. The total midgut protease activity was measured as described by
Sagili et al. (2005) (link)
. Briefly, frozen guts were crushed using a glass pestle, homogenized in Tris–HCl buffer (pH 7.9), and centrifuged at 10,000 rpm at 4°C for 5 min. The supernatants were used to determine the total midgut proteolytic enzyme activity (
Michaud et al. 1995 (link)
).
Twenty microliters of assay buffer (0.1 M Tris–HCl, pH 7.9) and 60 μl of 2% (w/v) azocasein diluted in assay buffer were added to 5 μl of supernatant. After 6 h of incubation at 37°C, the reaction was stopped by adding 300 μl of 10% (w/v) trichloroacetic acid to each mixture. The tubes were centrifuged for 5 min at 10,000 rpm, and 350 μl of the supernatant was added to 200 μl of 50% ethanol in water. The absorbance of this mixture was measured at 440 nm using a Shimadzu spectrophotometer (Model #UV-2450, Shimadzu Corporation). The total midgut proteolytic activity was expressed as OD
440.
9
Soil Enzyme Activities Analysis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The enzyme activities of urease, dehydrogenase and β-glucosidase were analyzed by using the colorimetric method (UV-VIS spectrophotometer, Model UV-2450, Shimadzu, Kiyoto, Japan) [53 ]. For the determination of urease activity, 5 g of moist soil was incubated at 37 °C for 12 h after adding (NH4+) released from a solution of urea (10%), and the control was processed by adding distilled water. Dehydrogenase activity was determined based on extraction with methanol (CH3OH) and the colorimetric determination of the triphenylformazan (TPF) made from the reduction of 2,3,5-triphenyltetrazolium chloride (TTC). β-glucosidase activity was determined based on the colorimetric determination of p-nitrophenyl released by β-glucosidase, and 1 g of air-dried soil was incubated for 1 h at 37 °C with a buffered PNG (p-nitrophenyl-β-d glucosidase) solution (pH 6.0) and toluene.
10
Perovskite Photoluminescence Characterization
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
PL measurements were performed at room temperature (RT) using free-space excitation and collection through a visible-near-infrared microscope objective (Nikon 20×, Nikon Corporation, Tokyo, Japan, NA = 0.40). The sample was excited via a 30 kHz picosecond pulsed diode laser (Master Oscillator Fibre Amplifier, Picoquant, Picoquant GmbH, Berlin, Germany, excitation wavelength at 355 nm, pulse width 50 ps, and power of 10 μW). The PL measurement was based on epifluorescence method. PL spectra were detected using AvaSpec-HERO spectrometer (Avantes BV, Apeldoorn, The Netherlands). The emission was then selected by a band filter at 500 ± 25 nm and detected by a single-photon avalanche photodiode (APD) connected to a time-correlated single-photon counting acquisition module (Edinburgh Instruments, TCC900, Edinburgh Instruments Ltd., Livingstone, United Kingdom). Absorption spectra of perovskite crystals were obtained using ultraviolet-visible (UV-vis) spectrometer (Shimadzu, Model UV-2450). PLQY measurements were carried out by placing the sample inside a Labsphere integrating sphere coupled to a Newton 920 Charge Coupled Device (Andor) through an optical fibre for photon counting. Cobolt 320 nm continuous-wave diode laser was used as an excitation source.
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!