TITLE:
Acid-Phosphorus Activity of Wheat Varieties Rhizobacteria of Uzbekistan
AUTHORS:
Zair Saatovich Shakirov, Iskandar Takhirovich Yakubov, Karomat Suvanqulovna Mamanazarova, Mardanov Ikrom Xasan Ugli, Xayrullaev Abdumalik
KEYWORDS:
Rhizobacteria, Phosphate Mobilization, Nitrogen Fixation, Acid Phosphatase, Wheat, Strains
JOURNAL NAME:
Agricultural Sciences,
Vol.14 No.8,
August
8,
2023
ABSTRACT: In this work, local strains of phosphate-solubilizing microorganisms were isolated and identified from the wheat rhizosphere and exogenous acid phosphatase enzymes of locally active phosphate- and potassium-mobilizing rhizobacteria belonging to the genera Escherichia, Rahnella, Bacillus, Enterobacter, Pseudomonas, and Pantoea were studied. The efficiency of the physiological properties of rhizobacteria is determined by the production of soluble phosphorus, and the amount of phosphorus depends on the activity and biomass of bacteria that secrete phosphorus. This is done by phosphate solubilizing bacteria, and the habitat ecosystem is enriched with beneficial micronutrients. In these studies, active rhizobacteria activity of acid phosphatase in nutrient liquid was studied at different temperatures. Optimum pH activity index and temperature variability of enzymes were determined. It should be noted that in the most active phosphate-solubilizing strains the maximum enzymatic activity was observed in the culture fluid of R. aquatilis strain 17, which produced 1.086 μmol p-nitrophenol μmol/min/ml. P. agglomerans 22, P. agglomerans 20 and Ps. kilonensis 32 cultures phosphatase activity was 0.143 - 0.680 p-nitrophenol μmol/min/ml. It should be noted that the phosphatase activity of bacteria belonging to the same genus and species was very different from each other. That is, the enzyme activity of Rahnella aquatilis strain 17 was 9 times higher than the enzyme activity of Rahnella aquatilis strain 9. The pH optimum of sour phosphatase enzymes in Rahnella aquatilis strain 16 was 6.0. The optimum temperature of acid phosphatase activity was 45˚C and 50˚C. The reason for this may be that the strains were isolated in different soil and climate conditions. When the acid phosphatase activity of R. aquatilis 3, 9, E. cloacae 8 and P. agglomerans 22 cultures was determined at a temperature of 45˚C, it was observed that the enzyme activity increased by 2 - 4 times. Es. hermannii 1, Ps. kilonensis 26 and B. simplex 28 bacteria acid phosphatase activity was not significantly affected by temperature rise.