ArticleScientific reports2022
Pullulanase with high temperature and low pH optima improved starch saccharification efficiency.
Article in Scientific reports, 2022. 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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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Effect of Pullulanase debranching freeze-thaw treatments and fatty acid on functional properties of yam starches.NPJ science of food · 2025Article
- Characterization of different isogenic mutants derived from improved strains ofBiochemistry and biophysics reports · 2025Article
- Combined metabolomics and electronic tongue technology elucidated the mechanisms of regulation of color-taste characteristics of Huangqin (Food chemistry: X · 2025Article
- Superior thermostability and divalent cation sensitivity of isoamylase CMI294C from Cyanidioschyzon merolae.Plant molecular biology · 2025Article
- Comparative analysis of navy bean starch nanoparticles prepared via ultrasound, enzymatic debranching, and their synergistic application.Scientific reports · 2025Article
- Synergistic Engineering of the Twin-Arginine Translocation (Tat) Pathway and Membrane Capacity Enhances Extracellular Production of Amylosucrase inMicroorganisms · 2025Article
- Secretory expression of amylosucrase in Bacillus licheniformis through twin-arginine translocation pathway.Journal of industrial microbiology & biotechnology · 2024Article
- Pullulanase: unleashing the power of enzyme with a promising future in the food industry.Frontiers in bioengineering and biotechnology · 2023Review
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pullulanase, a starch debranching enzyme, is required for the preparation of high glucose/maltose syrup from starch. In order to expand its narrow reaction conditions and improve its application value, Bacillus naganoensis pullulanase (PulA) was mutated by site-directed mutagenesis and the biochemical characteristics of the mutants were studied. The mutant PulA-N3 with mutations at asparagine 467, 492 and 709 residues was obtained. It displayed the activity maximum at 60 °C and pH 4.5 and exceeded 90% activities between 45 and 60 °C and from pH 4.0 to pH 5.5, which was improved greatly compared with wild-type PulA. Its thermostability and acidic pH stability were also remarkably improved. Its catalytic rate (k
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