Uv 2400

The reduction of silver ions to NPs was monitored by measuring UV–vis spectra at a resolution of 1 nm in the wavelength range of 200–800 nm and different time intervals (5–120 min) using Shimadzu UV‐2400, Japan. The shape and size of the Drac‐AgNPs were determined using a transmission electron microscopy (TEM) by Zeiss LEO 906 80 kV, Germany. The crystalline structure of the powdered Drac‐AgNPs was determined using an X‐ray diffraction (XRD) (APD 2000, ItalStructures, Italy) in the 2θ range of 20–80° worked at 40 kV and 30 mA with Cu K‐1 radiation. Fourier‐transform infrared spectroscopy (FTIR) spectra of AgNPs and D. kotschyi leaf infusion were recorded using an IR prestige‐21 Shimadzu spectrometer using the KBr pellet. The concentration of silver after digestion of the Drac‐AgNPs with HNO₃ was determined by the atomic absorption spectrometry (AAS) method (AA‐680, Shimadzu, Japan).

The total Chl in the leaves was extracted with 80% acetone. The extract was analyzed using a spectrophotometer (Shimadzu UV2400, Japan). The total Chl, Chl a, and Chl b contents were estimated with light absorption values of 470, 645 and 663nm, respectively, according to Porra et al. (1994) (link). The rice quality traits were measured as previously described (Su et al., 2011 (link)).

UV/Vis absorption spectra were recorded using a Shimadzu UV2400 or UV2450 spectrophotometer and an optical cell (width, 2 mm; light path, 1 cm). The sample temperature was maintained by a temperature controller (RTE-210, NESLAB) at 0 ± 0.1 °C. The sample was irradiated with light which was generated by a 1-kW tungsten halogen lamp (Master HILUX-HR, Rikagaku Seiki) and passed through optical filters (Y-52 or UV-D36C, AGC Techno Glass). The transient absorption spectra of Opn5m T188C mutant protein were recorded using a Shimadzu UV2450 spectrophotometer at 10 ± 0.1 °C. The spectra were measured in the dark and after 2 min irradiation with light which was generated by a 1-kW tungsten halogen lamp and passed through an optical filter (Y-52, AGC Techno Glass). The transient absorption spectra of Opn5m T188C mutant protein were also recorded using a high-speed CCD camera spectrophotometer (C10000 system, Hamamatsu Photonics) kept at 37 ± 0.1 °C by a temperature controller (qpod, QUANTUM Northwest)^{25 (link)} to accelerate the photocyclic reaction, according to the methods used in our previous study for Opn5L1^{18 (link)}. The flash light for irradiation was generated by a short-arc power flash (SA-200, Nissin Electronic; pulse duration of ~170 μs and flash lamp input of 200 J/F) and passed through an optical filter (Y-48, AGC Techno Glass).

UV/Vis absorption spectra were recorded using a spectrophotometer (UV2400, UV2450 or UV2600, Shimadzu) and an optical cell (width, 2 mm; light path, 1 cm). The sample temperature was maintained using a temperature controller (RTE-210, NESLAB) at 0 ± 0.1 °C. The sample was irradiated with light which was generated by a 1-kW tungsten halogen lamp (Master HILUX-HR, Rikagaku Seiki) and passed through an optical filter (Y-52, AGC Techno Glass).

The polysaccharide solution (1 mg mL⁻¹) was prepared and applied to ultraviolet spectral analysis. The UV scanning spectrum was measured in the wavelength range of 190–600 nm by spectrophotometer (UV-2400, Shimadzu, Japan).
The absorption spectrum of the IPCM-2 and EPCM-2 were obtained using FT-IR spectroscopy. 10 mg of the sample was thoroughly ground with KBr powder (100 mg). The dried mixture was then pressed into 1 mm thick pellets for FT-IR spectral analysis. The FT-IR spectra were recorded in a range of 4000–450 cm⁻¹ by an transmission infrared spectrometer (Sigma, USA).