Article3 Biotech2021
Engineering of thermostable phytase-xylanase for hydrolysis of complex biopolymers.
Article in 3 Biotech, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Influence of a Thermostable Fungal Xylanase Combined With Multi-Enzyme Complexes on the Structure, Physicochemical, and Functional Properties of Dietary Fiber From Hawthorn Pomace.Journal of food science · 2026Article
- Evaluating the nutritional impact of co-expressed phytase genes from Escherichia coli and Aspergillus niger in Pichia pastoris on broiler chickens.Tropical animal health and production · 2025Article
- Recent advances in phytase thermostability engineering towards potential application in the food and feed sectors.Food science and biotechnology · 2025Review
- pCold-assisted expression of a thermostable xylanase from3 Biotech · 2022Article
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
Industrial processing of enzymes requires higher heating that affects the thermal stability of the enzyme and increases the production cost. In this study, xylanase-phytase (XP) fusion protein was generated via co-expression in a single vector with a cold-shock promoter, leading to improved activity at optimal pH, temperature and the thermal behaviour of the protein. Xylanase-phytase (XP) fusion and phytase proteins were characterized by differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA). The XP fusion was thermally stable up to 124 °C, higher than phytase which was steady up to 113.5 °C. XP fusion exhibits higher stability at its thermal transition midpoint ( SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13205-021-02936-z.
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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.