ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2015
Isolation of a thermostable acid phytase from Aspergillus niger UFV-1 with strong proteolysis resistance.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Purification and biochemical characterization of Aspergillus niger NT7 phytase: Evaluation of its dephytinization potential under simulated digestion conditions.World journal of microbiology & biotechnology · 2025Article
- Production of Phytase byIndian journal of microbiology · 2025Article
- Production, purification and characterization of phytase from Pichia kudriavevii FSMP-Y17and its application in layers feed.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Review
- Production and characterization of a novel, thermotolerant fungal phytase from agro-industrial byproducts for cattle feed.Biotechnology letters · 2021Article
- Phytic Acid in Brown Rice Can Be Reduced by Increasing Soaking Temperature.Foods (Basel, Switzerland) · 2020Article
- Recovery and purification ofBiotechnology reports (Amsterdam, Netherlands) · 2020Article
- Production of Fungal Phytases from Agroindustrial Byproducts for Pig Diets.Scientific reports · 2019Article
- Article
- Characteristics of the First Protein Tyrosine Phosphatase with Phytase Activity from a Soil Metagenome.Genes · 2019Article
- Partial purification and characterization of phytase from Aspergillus foetidus MTCC 11682.AMB Express · 2019Article
- Purification and biochemical characterization of anBiotechnology reports (Amsterdam, Netherlands) · 2018Article
- New Bacterial Phytase through Metagenomic Prospection.Molecules (Basel, Switzerland) · 2018Article
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4 authors at 1 institution in 1 country.
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Abstract
An Aspergillus niger UFV-1 phytase was characterized and made available for industrial application. The enzyme was purified via ultrafiltration followed by acid precipitation, ion exchange and gel filtration chromatography. This protein exhibited a molecular mass of 161 kDa in gel filtration and 81 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), indicating that it may be a dimer. It presented an optimum temperature of 60 °C and optimum pH of 2.0. The K M for sodium phytate hydrolysis was 30.9 mM, while the k cat and k cat / K M were 1.46 ×10 (5) s (-1) and 4.7 × 10 (6) s (-1) .M (-1) , respectively. The purified phytase exhibited broad specificity on a range of phosphorylated compounds, presenting activity on sodium phytate, p-NPP, 2- naphthylphosphate, 1- naphthylphosphate, ATP, phenyl-phosphate, glucose-6-phosphate, calcium phytate and other substrates. Enzymatic activity was slightly inhibited by Mg (2+) , Cd (2+) , K (+) and Ca (2+) , and it was drastically inhibited by F (-) . The enzyme displayed high thermostability, retaining more than 90% activity at 60 °C during 120 h and displayed a t 1/2 of 94.5 h and 6.2 h at 70 °C and 80 °C, respectively. The enzyme demonstrated strong resistance toward pepsin and trypsin, and it retained more than 90% residual activity for both enzymes after 1 h treatment. Additionally, the enzyme efficiently hydrolyzed phytate in livestock feed, liberating 15.3 μmol phosphate/mL after 2.5 h of treatment.
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