ArticleApplied and environmental microbiology2002
Engineering of phytase for improved activity at low pH.
Article in Applied and environmental microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 100 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
- Catalytic Residue Reprogramming Enhances Enzyme Activity at Alkaline pH via Phenolate-Mediated Proton Transfer.ACS synthetic biology · 2025Article
- Primary high-throughput screening of engineered phytases by online monitoring of the oxygen transfer rate of Komagataella phaffii.Microbial cell factories · 2025Article
- Powerful cell wall biomass degradation enzymatic system from saprotrophicCell surface (Amsterdam, Netherlands) · 2024Review
- Characterisation of a soil MINPP phytase with remarkable long-term stability and activity from Acinetobacter sp.PloS one · 2022Article
- Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris.Biotechnology for biofuels · 2021Article
- Effect of Polar Amino Acid Residue Substitution by Site-Directed Mutagenesis in the N-terminal Domain ofJournal of microbiology and biotechnology · 2020Article
- Creating Oxidase-Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions.Chembiochem : a European journal of chemical biology · 2017Article
- Identification of a phosphinothricin-resistant mutant of rice glutamine synthetase using DNA shuffling.Scientific reports · 2015Article
- Phosphoryl transfer from α-d-glucose 1-phosphate catalyzed by Escherichia coli sugar-phosphate phosphatases of two protein superfamily types.Applied and environmental microbiology · 2015Article
- Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase fromBiotechnology reports (Amsterdam, Netherlands) · 2014Article
- Article
- Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.Applied and environmental microbiology · 2012Article
- Improvement of glyphosate resistance through concurrent mutations in three amino acids of the Ochrobactrum 5-enopyruvylshikimate-3-phosphate synthase.Applied and environmental microbiology · 2011Article
- Enzymes in food processing: a condensed overview on strategies for better biocatalysts.Enzyme research · 2010Article
- Production of feed enzymes (phytase and plant cell wall hydrolyzing enzymes) by Mucor indicus MTCC 6333: purification and characterization of phytase.Folia microbiologica · 2007Article
- Production and biochemical characterization of insecticidal enzymes from Aspergillus fumigatus toward Callosobruchus maculatus.Current microbiology · 2006Article
- Shifting the pH profile of Aspergillus niger PhyA phytase to match the stomach pH enhances its effectiveness as an animal feed additive.Applied and environmental microbiology · 2006Article
- Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum.Applied and environmental microbiology · 2005Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For industrial applications in animal feed, a phytase of interest must be optimally active in the pH range prevalent in the digestive tract. Therefore, the present investigation describes approaches to rationally engineer the pH activity profiles of Aspergillus fumigatus and consensus phytases. Decreasing the negative surface charge of the A. fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowered the pH optimum by ca. 0.5 unit but also resulted in 70 to 75% inactivation of the enzyme. Alternatively, detailed inspection of amino acid sequence alignments and of experimentally determined or homology modeled three-dimensional structures led to the identification of active-site amino acids that were considered to correlate with the activity maxima at low pH of A. niger NRRL 3135 phytase, A. niger pH 2.5 acid phosphatase, and Peniophora lycii phytase. Site-directed mutagenesis confirmed that, in A. fumigatus wild-type phytase, replacement of Gly-277 and Tyr-282 with the corresponding residues of A. niger phytase (Lys and His, respectively) gives rise to a second pH optimum at 2.8 to 3.4. In addition, the K68A single mutation (in both A. fumigatus and consensus phytase backbones), as well as the S140Y D141G double mutation (in A. fumigatus phytase backbones), decreased the pH optima with phytic acid as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity. These findings significantly extend our tools for rationally designing an optimal phytase for a given purpose.
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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.