KINETIC CHARACTERIZATION OF ACID PHOSPHATASE OF Enterobacter sp. ISOLATED FROM ORCHID
DOI:
https://doi.org/10.63330/aurumpub.012-044Keywords:
Phosphorus solubilization, Rhizobacteria, Microbial enzymes, PhosphomonohydrolasesAbstract
Phosphorus is an essential nutrient for plant growth, but its availability in soil is often limited due to the predominance of insoluble organic forms. Root-associated microorganisms, such as plant growth-promoting bacteria (PGPR), play a crucial role in phosphorus solubilization through the production of hydrolytic enzymes, such as phosphatases. This study aimed to kinetically characterize the acid phosphatase produced by a strain of Enterobacter sp. (C45), isolated from the roots of the orchid Cyrtopodium paludicolum. The enzyme was produced in culture media with different phosphate concentrations, with maximum activity observed at 5 mM. The phosphatase exhibited an apparent optimum pH of 3.5 and demonstrated the ability to hydrolyze various phosphorylated substrates, such as p-nitrophenylphosphate (p-NFF), ATP, and pyrophosphate, with Michaelian kinetics for p-NFF and positive cooperativity for the others. Inhibition studies revealed sensitivity to metals (Cu²⁺) and phosphate analogs (arsenate, vanadate), with competitive and non-competitive inhibition modes. The enzyme demonstrated thermal stability up to 45°C, with rapid inactivation at higher temperatures. The results indicate that acid phosphatase from Enterobacter sp. has distinctive catalytic properties and biotechnological potential for application in phosphorus solubilization processes under acidic conditions, such as in sustainable agriculture and the animal feed industry.
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