To assess the total carotenoid content, carotenoids were extracted from the crude, dried, and roasted avocado seeds, using ethanol: ethyl acetate: petroleum ether (1:1:1, v/v/v). Successive extractions were performed. The extracts were combined, filtered, and washed with distilled water, diethyl ether, and a saturated solution of NaOH. The ethereal phase was recovered and subjected to rotary evaporation at 35 °C (Heidolph Rotary Evaporator, Schwabah, Germany). Estimation of carotenoids was spectrophotometrically determined using Shimadzu UV-VIS 1700 set at 450 nm (Shimadzu, Kyoto, Japan).
Uv vis 1700
Manufactured by Shimadzu
Sourced in Japan
The UV-VIS 1700 is a double-beam, single-monochromator spectrophotometer designed for a wide range of UV-VIS absorption measurements. It features a wavelength range of 190 to 1100 nm, with a spectral bandwidth of 1.0 nm. The instrument uses a deuterium lamp for the UV region and a halogen lamp for the visible region.
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Lab products found in correlation
10 protocols using uv vis 1700
1
Carotenoid Extraction from Avocado Seeds
2
Lamivudine-Loaded Microsphere Entrapment Efficiency
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The drug‐loaded microspheres (100 mg) were powdered and suspended in 100 ml of the acetone–ethanol mixture, and 6 ml of acetonitrile was added and vortexed for 5 min. The drug content was determined by measuring the absorbance at 261 nm using a UV–Vis spectrophotometer (Shimadzu, UV‐Vis 1700, Japan). The efficiency of drug trapping was determined with the following equation.
All the formulations were analysed in triplicate (n = 3).
All the formulations were analysed in triplicate (n = 3).
3
Superoxide Anion Scavenging Assay for AQDL
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The superoxide anion radicals scavenging action of AQDL was determined based on the modified procedure of Liu et al. [31 (link)] as described in detail by Kamisan et al. [23 (link)]. According to this modified procedure, the superoxide radicals were generated in phenazine methosulphate-nicotinamide adenine dinucleotide (PMS-NADH) systems through the oxidation of NADH and measured based on the reduction of nitroblue tetrazolium (NBT). Briefly, the reaction mixture containing the superoxide radicals was prepared by mixing 3 mL of Tris-HCl buffer (16 mM, pH 8) containing 1 mL of NBT (50 μM), 1 mL NADH (78 μM) and AQDL (25–50 μg) with 1 mL of phenazine methosulphate (PMS) solution (10 μM). The reaction mixture was then incubated at 25 °C for 5 min followed by the absorbance measurement at 560 nm using a spectrophotometer (UV–vis 1700, Shimadzu, Japan). Changes in the absorbance were compared between the AQDL-treated reaction mixtures against blank control or L-ascorbic acid as the positive control, and a decrease in the recorded absorbance indicates increasing superoxide anion scavenging activity. The percentage inhibition of superoxide anion production was evaluated using the following equation:
where AC was the absorbance of the blank control and AT was the absorbance in the presence of AQDL or positive control.
where AC was the absorbance of the blank control and AT was the absorbance in the presence of AQDL or positive control.
4
SOA Radical Scavenging Activity Protocol
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The SOA radical scavenging activity was determined according to Liu et al. [10 (link)] but with slight modification. A mixture of 3 mL of Tris-HCl buffer (16 mM, pH 8), 1 mL of NBT (50 μM), 1 mL NADH (78 μM), and each of the respective partition (25–50 μg) was first prepared. The reaction was initiated by adding 1 mL of PMS solution (10 μM) and the mixture solution was incubated at 25°C for 5 min. The activity was read at absorbance 560 nm using a spectrophotometer (Shimadzu UV-Vis 1700) against blank samples and using l-ascorbic acid as a control.
5
Ferric Reducing Antioxidant Power Assay
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The FRAP values of mice plasma were determined according to Benzie and Strain, 1996 [32 (link)], with some modification. All reagents were prepared and used the same day. The working FRAP reagent was prepared by mixing in ratio 10:1:1 (v/v/v) of 300 mM acetate buffer (pH 3.6), 10 mM TPTZ (2,4,6-tripyridyl-s-triazine) in 40 mM HCl and 20 mM FeCl3·6H2O. Briefly, a 50 µL sample was mixed with 150 µL distilled water and 1.5 mL working FRAP solution. After 30 min, the absorbance at 595 nm was measured against a reagent blank at 37 °C using The PharmaSpec Shimadzu UV–Vis 1700 (Shimadzu, Kyoto, Japan) spectrophotometer. The FRAP values were expressed as mmol FeSO4/L by using different concentrations of aqueous solutions of FeSO4·7H2O (in the range of 50–1000 µM) for a standard curve.
6
Enzymatic Activity Profiling of Apple Fruit
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Apple fruit samples were ground in liquid nitrogen before being measured for their activities of the contained enzymes PPO (BC0190), POD (BC0090), LOX (BC0320), PLD (BC2415), SOD (BC0170), catalase (CAT) (BC0205), ascorbate peroxidase (APX) (BC0220), and glutathione S-transferase (GST) (BC0350) using the corresponding assay kits (Solarbio Inc. Beijing, China) in accordance with the manufacturer’s instructions. The activities of PPO, POD, LOX, PLD, SOD, CAT, APX, and GST were determined by a spectrophotometer (UV-Vis 1700, Shimadzu, Columbia, MD, USA) at 410 nm, 470 nm, 280 nm, 290 nm, 560 nm, 240 nm, 510 nm, and 340 nm, respectively. Enzyme activity units (U) were expressed as U g−1 per fresh weight (FW). All experiments were performed with three independent biological replicates.
7
Serum Biochemistry in Rabbits
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Blood was collected after 7 and 14 days in the afternoon from a venipuncture jugular vein at fed state without any anaesthetic agent. The rabbits were weighted and slaughtered after 7 days; different organs were collected, that is, heart, kidneys, and liver, and stored in 10% formalin solution. Standard procedures of reagent of HUMAN (HUMAN, Germany) were applied for biochemical tests using UV-Spectrophotometer (UV-vis 1700; Shimadzu, Japan). Glucose and SGPT level were also determined using Merck's reagent kits (Merck, Germany).
8
DPPH Radical Scavenging Assay for Antioxidant Evaluation
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The method proposed by Diaconeasa et al. [27 (link)], with some modifications, allowed the estimation of the free radical reduction capacity using a solution of 2,2-diphenyl-1-picrilhydrazyl (DPPH) and was adapted to evaluate the antioxidant activity of the different ripening elder extracts. A total of 100 µL of the methanolic extract of the samples was added to the 3.9 mL DPPH solution (0.025 g/L) to be analyzed. The mixture was properly homogenized, and kept in the dark for 30 min. The absorbance of the samples was recorded at 515 nm (UV-VIS 1700 Shimadzu). The control solution was prepared according to the same protocol but replaced the 100 μL of sample (methanolic extract) with methanol. The results were evaluated as a percentage of the inhibition capacity, based on the following equation: DPPH scavenging effect (%) = [(Ac − AP) × 100]/Ac], where: Ac—absorbance of the control solution (nm); AP—sample absorbance (nm).
9
Cultivation and Inoculation of E. coli K12
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Stock cultures of E. coli K12 MG1655 (henceforth E. coli) were maintained on Luria-Bertani (LB) agar plates (containing 10 g peptone, 10 g NaCl, 5 g yeast extract and 2% (w/v) agar in 1000 ml distilled water) at 30°C. To develop the inoculums, a single colony of E. coli from the LB agar plate was inoculated into LB broth (LB agar minus agar) and incubated for growth under shaking at 150 r.p.m and at 30°C. E. coli growth was monitored by measuring absorbance at 600 nm using a spectrophotometer (Shimadzu UV-VIS 1700, North America). E. coli grown to a OD of 0.8 (106 CFU/ml) was used as inoculum for all the experiments unless otherwise mentioned.
10
Laccase Activity Assay Using SGZ and CuSO4
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The assay mixture consisted of 10 μL of appropriately diluted LacAn stock and 990 μL of 50 mM Na 2 HPO 4 -KH 2 PO 4 buffer (pH 7.0) containing 100 μM SGZ (65, 000 M -1 cm -1 ) and 10 μM CuSO 4 . The reaction was initiated by adding SGZ and enzyme into the solution. After incubation at 45 °C for 5 min, the mixture was transferred into ice-water bath for 30 s to stop the reaction and the absorbance was measured at 525 nm using a UV-visible spectrophotometer (Shimadzu uv-vis 1700, Japan). Alternative substrates for the measurement of laccase activity were 2 mM 2,6-DMP. Reactions with heat-treated LacAn were used as control. One activity unit (U) was defined as the amount of LacAn for oxidizing 1 μmol of substrate per minute. Protein concentration of LacAn was determined at 595 nm using the Modified Bradford Protein Assay Kit (Sangon, China) as bovine serum albumin as the standard.
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