Article3 Biotech2016
Phytases from Enterobacter and Serratia species with desirable characteristics for food and feed applications.
Article in 3 Biotech, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
8 citing papers in PubMed, 51 citations in OpenAlex.
- Genomic prediction of phytase potential and stress tolerance in maize-associated plant growth-promoting rhizobacterium Enterobacter cloacae Mz49.AMB Express · 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 on Desirable Microbial Phytases as a Poultry Feed Additive: Their Sources, Production, Enzymatic Evaluation, Market Size, and Regulation.International journal of microbiology · 2024Review
- Exploring the biotechnological potential of novel soil-derivedFrontiers in bioengineering and biotechnology · 2024Article
- Microbial Phytases: Properties and Applications in the Food Industry.Current microbiology · 2023Review
- Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153).Molecular biotechnology · 2018Article
- Article
- Regulation of Soluble Phosphate on the Ability of Phytate Mineralization and β-Propeller Phytase Gene Expression of Pseudomonas fluorescens JZ-DZ1, a Phytate-Mineralizing Rhizobacterium.Current microbiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phytases are enzymes of great industrial importance with wide range of applications in animal and human nutrition. These catalyze the hydrolysis of phosphomonoester bonds in phytate, thereby releasing lower forms of myo-inositol phosphates and inorganic phosphate. Addition of phytase to plant-based foods can improve its nutritional value and increase mineral bioavailability by decreasing nutritional effect of phytate. In the present investigation, 43 phytase positive bacteria on PSM plates were isolated from different sources and characterized for phytase activity. On the basis of phytase activity and zone of hydrolysis, two bacterial isolates (PSB-15 and PSB-45) were selected for further characterization studies, i.e., pH and temperature optima and stability, kinetic properties and effect of modulators. The phytases from both isolates were optimally active at the pH value from 3 to 8 and in the temperature range of 50-70 °C. Further, the stability of isolates was good in the pH range of 3.0-8.0. Much variation was observed in temperature and storage stability, responses of phytases to metal ions and modulators. The K
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.