ArticleMolecular biotechnology2018
Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153).
Article in Molecular biotechnology, 2018. 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, 50 citations in OpenAlex.
- Development of a Gold Nanoparticle-Assisted Multiplex Polymerase Chain Reaction Assay for Selected Hospital-Acquired Infections-Associated Bacterial and Fungal Pathogens.ChemistryOpen · 2026Article
- Functional Benefits of Brewer's Spent Grain and the Challenge of Developing Food Ingredients for Human Health.Antioxidants (Basel, Switzerland) · 2026Review
- Investigation of Probiotic Properties ofFood science & nutrition · 2025Article
- EvaluatingFood science & nutrition · 2024Article
- Review on Desirable Microbial Phytases as a Poultry Feed Additive: Their Sources, Production, Enzymatic Evaluation, Market Size, and Regulation.International journal of microbiology · 2024Review
- Purification and biochemical characterization of phytase from Bacillus cereus isolated from gastrointestinal tract of African giant snail (Achatina fulica).International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Barley Nepenthesin-Like Aspartic ProteaseFrontiers in plant science · 2021Article
- Probiotic properties of a phytase producing Pediococcus acidilactici strain SMVDUDB2 isolated from traditional fermented cheese product, Kalarei.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, minerals, phosphorus and energy. In the present study, phytase isolation from the Lactobacillus coryniformis strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca
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