OD660 was assayed at 660 nm using the spectrophotometer (UV-560, JASCO, Japan). The concentrations of nitrate and nitrite were determined according to the standard methods (Zhang et al. 2015 (link)). Cobalt(II) concentration was determined by spectrophotometry (UV-560, JASCO, Japan) according to the method used by Long et al. (2017 (link)). Biomass growth was quantified by measuring the bacterial protein concentration in the reaction system according to the Bradford procedure (Bradford 1976 (link)). Fe(II) concentration was determined according to the method used by Dong et al. (2013 (link)). The dissolved oxygen was measured by dissolved oxygen analyzer (Rex JPBJ-608, Shanghai INESA, China). A pH meter (EL20, Shanghai Mettler-Toledo, China) was used to measure pH values. Gas samples were determined by a gas chromatography (GC7900, Techcomp, China) equipped with a thermal conductivity detector, a Porapak Q and a Molecular Sieve column. Helium was used as the carrier gas with a flow of 30 mL/min. The temperatures were 50 °C for the column, 120 °C for the detector and 120 °C for the injection port.
Uv 560
Manufactured by Jasco
Sourced in Japan
The UV-560 is a high-performance ultraviolet-visible spectrophotometer. It is designed to measure the absorption of light by various samples within the ultraviolet and visible light spectrum.
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Lab products found in correlation
3 protocols using uv 560
1
Analytical Methods for Microbial Growth and Metabolite Quantification
2
Enzyme Activity Assays for Bioremediation
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The protein concentration in the crude enzyme solution was determined by the Bradford method (Bradford, 1976) (link). The method of PheA assay mainly consisted of a reaction substrate consisting of 50 mM Tris-HCl buffer (pH 8.0) containing 2.5 mM phenol and 1 mol L -1 NADH. 1mL of reaction substrate was added to 100 μL of enzyme extract and incubated at 30 °C for 30 min at constant temperature. The initial and nal absorbance was measured at 340 nm using a UV-vis spectrophotometer (JASCO, UV-560, Japan).
The catechol 1,2-dioxygenase activity assay (C12O) and catechol 2,3-dioxygenase activity assay (C23O) were performed with reference to the methods in the literature (Mahiudddin, et al., 2012 (link); Nakazawa, T. and Nakazawa, A., 1970;), absorbance was read at 260 nm and 375 nm, respectively. The speci c activity is the number of units of enzyme activity per mg of cellular protein.
The catechol 1,2-dioxygenase activity assay (C12O) and catechol 2,3-dioxygenase activity assay (C23O) were performed with reference to the methods in the literature (Mahiudddin, et al., 2012 (link); Nakazawa, T. and Nakazawa, A., 1970;), absorbance was read at 260 nm and 375 nm, respectively. The speci c activity is the number of units of enzyme activity per mg of cellular protein.
3
Spectrophotometric Determination of Redox Cofactors
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UV-Vis spectra were measured using a double beam spectrophotometer (UV-560, JASCO, Japan).
Protein and substrate concentrations were determined from the extinction coefficients: CtFNRox, ε466 = 10.3 mM -1 cm -1 (Seo and Sakurai 2002) and NADPH and NADPD, ε340 = 6.2 mM -1 cm -1 . NADP + concentration was determined in NADPH form using glucose-6-phosphate dehydrogenase and excess amount of glucose-6-phosphate.
Protein and substrate concentrations were determined from the extinction coefficients: CtFNRox, ε466 = 10.3 mM -1 cm -1 (Seo and Sakurai 2002) and NADPH and NADPD, ε340 = 6.2 mM -1 cm -1 . NADP + concentration was determined in NADPH form using glucose-6-phosphate dehydrogenase and excess amount of glucose-6-phosphate.
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