ArticlePloS one2018
Improvement of bread making quality by supplementation with a recombinant xylanase produced by Pichia pastoris.
Article in PloS one, 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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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.
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Who cites it
8 citing papers in PubMed, 51 citations in OpenAlex.
- Production of Xylooligosaccharides (XOSs) with Anti-inflammatory and Prebiotic Activities Using Recombinant Endo-1,4-β-xylanases fromJournal of agricultural and food chemistry · 2026Article
- BioengineeringMicroorganisms · 2025Article
- Insight into the eminent biotechnological applications of xylanolytic enzymes for sustainable bioprocessing.3 Biotech · 2025Review
- Improving the Quality of Wheat Flour Bread by a Thermophilic Xylanase with Ultra Activity and Stability Reconstructed by Ancestral Sequence and Computational-Aided Analysis.Molecules (Basel, Switzerland) · 2024Article
- Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017.Molecular biotechnology · 2022Article
- Article
- Purification and characterization of two thermostable xylanases from a halotolerant Bacillus sp. Asc6BA isolated from Salar de Ascotán, Atacama Desert.Extremophiles : life under extreme conditions · 2021Article
- Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins.Journal of cellular physiology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Xylanases (EC 3.2.1.8) are hydrolytic enzymes, which randomly cleave the β-1,4-linked xylose residues from xylan. The synthetic gene xynBS27 from Streptomyces sp. S27 was successfully cloned and expressed in Pichia pastoris. The full-length gene consists of 729 bp and encodes 243 amino acids including 51 residues of a putative signal peptide. This enzyme was purified in two steps and was shown to have a molecular weight of 20 kDa. The purified r-XynBS27 was active against beechwood xylan and oat spelt xylan as expected for GH 11 family. The optimum pH and temperature values for the enzyme were 6.0 and 75 °C, respectively. The Km and Vmax were 12.38 mg/mL and 13.68 μmol min/mg, respectively. The r-XynBS27 showed high xylose tolerance and was inhibited by some metal ions and by SDS. r-XynBS27 was employed as an additive in the bread making process. A decrease in firmness, stiffness and consistency, and improvements in specific volume and reducing sugar content were recorded.
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Registered trials
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