Key message Ca 2+ NPs enhanced tolerance of Triticale callus under salt stress by improving biochemical activity and confocal laser scanning analysis, conferring salt tolerance on callus cells. Abstract CaO NPs (Ca 2+ ) are significant components that act as transducers in many adaptive and developmental processes in plants. In this study, effect of Ca 2+ NPs on the response and regulation of the protective system in Triticale callus under short and long-salt treatments was investigated. The activation of Ca 2+ NPs was induced by salt stress in callus of Triticale cultivars. MDA, H 2 O 2 , POD, and protein activities were determined in callus tissues. Concerning MDA, H 2 O 2 , protein activities, it was found that the Ca 2+ NPs treatment was significant, and it demonstrated a high correlation with the tolerance levels of cultivars. Tatlıcak cultivar was detected for better MDA activities in the short time with 1.5 ppm Ca 2+ NPs concentration of 50 g and 100 g NaCl. Similarly, the same cultivar responded with better H 2 O 2 activity at 1.5 ppm Ca 2+ NPs 100 g NaCl in the short time. POD activities exhibited a decreasing trend in response to the increasing concentrations of Ca 2+ NPs. The best result was observed at 1.5 ppm Ca 2+ NPs 100 g NaCl in the short term. Based on the protein content, treatment of short-term cultured callus cells with 1.5 ppm Ca 2+ NPs inhibited stress response and it significantly promoted Ca 2+ NPs signals as compared to control callus. Confocal laser scanning analysis proved that the application of Ca 2+ NPs could alleviate the adverse effects of salt stress by the inhibition of stress severity in callus cells. This study demonstrated, under in vitro conditions, that the application of Ca 2+ NPs can significantly suppress the adverse effects of salt stress on Triticale callus; it was also verified that the concentration of Ca 2+ NPs could be important parameter to be considered in adjusting the micronutrient content in the media for this plant.
The remediation of methylene blue from wastewater using chitosan-sunflower-nano-iron (CSN) beds was examined in this study with the Fenton process. Nano-iron is synthesized using the green synthesis process. Then, biopolymer beds obtained nano-iron, sunflower tray waste, and chitosan. These beds used the Fenton process for removing Methylene blue (MB) from water. Beds synthesis and dye removing are characterized using SEM, TEM, FTIR, and XRD techniques. For the method optimization, the effects of dye concentration, temperature, pH, H2O2, and amount of biocatalyst were studied. The result of the wavelength scan was found 660 nm for methylene blue dye. Using CSN, catalyst was very effective in color removal for MB under optimal conditions. The highest removal rate 98% was obtained at pH 6 for 270 min. The optimum conditions for the MB dye are as follows; dye concentration: 25 mg/L, amount of absorbent: 2.5 mg/mL, temperature: 60 °C, H2O2 amount: 20 mg/L (600 µL, 30%). When the experiment is studied in optimum conditions, max. dye removal was calculated to be 98%. From SEM, TEM, XRD, and FTIR results, the change in the surface of the biocatalyst could be clearly observed. It is understood that the biocatalyst synthesized from the results we obtained easily removed a large amount of dye (MB).
In this research, protease enzyme was purified and characterized from milk of Euphorbia amygdaloides. (NH4)2SO4 fractionation and CM-cellulose ion exchange chromatography methods were used for purification of the enzyme. The optimum pH value was determined to be 5, and the optimum temperature was determined to be 60 degrees C. The V(max) and K(M) values at optimum pH and 25 degrees C were calculated by means of Linewearver-Burk graphs as 0.27 mg/L min(-1) and 16 mM, respectively. The purification degree was controlled by using SDS-PAGE and molecular weight was found to be 26 kD. The molecular weight of the enzyme was determined as 54 kD by gel filtration chromatography. These results show that the enzyme has two subunits. In the study, it was also researched whether purified and characterized protease can be collapsed to milk. It was determined that protease enzyme can collapse milk and it can be used to produce cheese.
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