ArticleMolecular biotechnology2022
Response Surface Methodology Based Optimization, Partial Purification and Characterization of Alkaline Phosphatase Isolated from Pseudomonas asiatica Strain ZKB1 and its Application in Plant Growth Promotion.
Article in Molecular biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Biochemical and biological evaluation of L-glutaminase from Aspergillus tamarii AUMC 10198 via solid-state fermentation.Microbial cell factories · 2025Article
- Anticancer, antioxidant and antibacterial potential of L-Glutaminase (Streptomyces roseolus strain ZKB1) capped silver and zinc oxide nanoparticles and its molecular characterization.Bioresources and bioprocessing · 2025Article
- Development and mechanism exploration of a quantitative model for Escherichia coli transformation efficiency based on ultrasonic power.Ultrasonics sonochemistry · 2024Article
- Phosphate-Solubilizing Bacteria: Advances in Their Physiology, Molecular Mechanisms and Microbial Community Effects.Microorganisms · 2023Review
- Optimization of subtilisin production fromSaudi journal of biological sciences · 2023Article
- Response surface methodology based optimization of keratinase fromSaudi journal of biological sciences · 2023Article
- Genomic Analysis ofGenes · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The present study was defined to evaluate the effect of a combinational approach of applying phosphate-solubilizing bacteria and alkaline phosphatase for plant growth promotion as a novel strategy. An extracellular phosphatase producing novel Pseudomonas asiatica strain ZKB1 was isolated from ant hill soil. Alkaline phosphatase production was statistically optimized by Plackett-Burman and central composite designs with a yield of 42.45 U/ml and 5.88-fold enhancement. Alkaline phosphatase was purified by column chromatography (DEAE-Cellulose and Sephadex G-100) with 17.55-fold purification and specific activity of 87.77 U/mg. The molecular mass of purified phosphatase was ~ 45 kDa. The optimum pH and temperature were 9.0 and 50 °C, respectively, revealing alkali-thermostability. Phosphatase exhibited the highest specificity toward p-nitrophenyl phosphate disodium salt. Kinetic analysis revealed K
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