Dialysis bags (Spectra/Por® membranes, MWCO 3.5 kDa) were filled with 1 mL of berberine loaded nanogel formulation (NG6L) and immersed in 12 mL NaCl 0.9% w/v. The systems were maintained under magnetic stirring (500 rpm) at 37 °C up to 24 h. Release medium (1 mL) was sampled at different time points and fresh saline solution (1 mL) was added to the system. Collected samples were analyzed using UH5300 UV-Visible Spectrophotometer (Hitachi, Chiyoda, Japan) at 345 nm and calibration curve built in the range 5–25 µg/mL (R2 = 0.9994). Blank nanogel formulation (NG6B) was used as control. Release studies were performed in triplicate using the same formulation batch.
Uh5300 uv visible spectrophotometer
Manufactured by Hitachi
Sourced in Japan
The UH5300 UV-Visible Spectrophotometer is a laboratory instrument designed to measure the absorption or transmission of light in the ultraviolet and visible regions of the electromagnetic spectrum. It is capable of performing various spectroscopic analyses on liquid, solid, or gaseous samples.
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Lab products found in correlation
6 protocols using uh5300 uv visible spectrophotometer
1
In Vitro Release of Berberine-Loaded Nanogels
2
Alginate Lyase Activity Quantification
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Alginate lyases degrade alginate by the β-elimination mechanism and generate a double bond between C4 and C5 of the sugar ring at the newly formed non-reducing end that can be monitored as a change in absorbance at 235 nm. Enzyme activity was determined with 100 μL of enzyme solution and 900 μL of substrate solution (0.3% (w/v) sodium alginate, 20 mM phosphate buffer, 500 mM NaCl, pH 7.3) at 30 °C for 10 min. Absorbance measurements were taken by UH5300 UV-visible spectrophotometer (HITACHI, Japan). One unit (U) was defined as the amount of enzyme required to increase the absorbance at 235 nm by 0.1 per min [13 (link)]. In each experiment, pre-experiments were done to adjust the protein concentration and keep the value within the credible A235 range from 0.2 to 1.5.
3
Quantification of FA-loaded Nanofibers
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Approx. 2 mg of FA-loaded nanofibers were immersed in 1 mL of MilliQ water for 5 min. Then, solutions were 20-fold diluted in MilliQ water and the absorbance recorded at 290 nm (UH5300 UV-Visible Spectrophotometer Hitachi, Chiyoda, Japan) for drug quantification. The experiments were carried out in triplicate.
4
Spectrophotometric Assay of Hyaluronidase
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The enzyme activity was measured in a 1 ml reaction system under the optimal reaction condition. First, 0.1 ml enzyme (0.18 U/ml) was added to 0.9 ml 0.2% (w/v) HA substrate solution. After incubation for 10 min at the optimal temperature, the reaction was terminated by boiling for 10 min, and then the absorbance of the solution was measured at 232 nm by a UH5300 UV visible spectrophotometer (HITACHI, Japan). One unit of enzyme activity was defined as the amount of the protein required to produce 1 μmol unsaturated oligosaccharides using the molecular extinction coefficient value of 5,500 M−1 cm−1 at 232 nm (Lin et al., 1994 (link)).
5
Solubility Study of RSV and MEL in Oils
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Solubility studies were performed by UV spectroscopy (UH5300 UV–visible spectrophotometer, Hitachi, Chiyoda, Japan) to evaluate the solubility of RSV and MEL in different oils (see Section 2.1 ). An excess amount of RSV was added to 1 mL of each oil and mixed for 24 h at room temperature (r.t.). Samples were then centrifuged at 25 °C for 1 h at 10,000 rpm. The supernatant was separated, and RSV was quantified after appropriate dilutions with methanol, using a standard calibration curve at λ = 306 nm, which was linear in the concentration range 1.527–20.36 μg/mL (R2 = 0.9992). The same procedure was adopted for MEL, which was quantified in the samples against a standard calibration curve at λ = 224 nm, which was linear in the range of concentrations 12.844–0.803 μg/mL (R2 = 0.9985).
6
Quantifying Alginate Lyase Activity
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Alginate lyase activity was determined by UV spectrophotometry for its change at 235 nm. Briefly, 900 μL of 0.3% (w/v) of alginate substrate (50 mM PB, 100 mM NaCl, pH 9.1) was incubated at 30 °C for 5 min, and then 100 μL of enzyme solution was added. Enzyme boiled at 100 °C for 10 min was used as the control. The A235 value was detected by UH5300 UV–visible spectrophotometer (HITACHI, Tokyo, Japan) after being incubated at 30 °C for 10 min. An enzyme activity unit (U) was defined as the amount of enzyme required to increase 0.1 units of UV absorption per minute. These results were repeated 3 times and the average values were indicated along with a standard deviation.
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