Article3 Biotech2016
Purification and characterization of polygalacturonase from Aspergillus fumigatus MTCC 2584 and elucidating its application in retting of Crotalaria juncea fiber.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Pectinase-Based Bioprocesses for Circular Bioeconomy and Sustainable Industrial Development.Biotechnology and bioengineering · 2026Review
- Bioconversion of wheat and bean straw by thermo-alkaliphilic actinomycetes for enhanced polygalacturonase yield: statistical optimization and industrial application.Biodegradation · 2026Article
- Thermostable and organic solvent-tolerant acid pectinase from3 Biotech · 2021Article
- An Exo-Polygalacturonase Pgc4 Regulates Aerial Hyphal Growth and Virulence inInternational journal of molecular sciences · 2020Article
- Pectinolytic Bacterial Consortia Reduce Jute Retting Period and Improve Fibre Quality.Scientific reports · 2020Article
- Overexpression and Biochemical Characterization of an Endo-α-1,4-polygalacturonase fromInternational journal of molecular sciences · 2020Article
- Enzymatic treatment of flax for use in composites.Biotechnology reports (Amsterdam, Netherlands) · 2018Review
- Microparticle-enhanced polygalacturonase production by wild type3 Biotech · 2017Article
- Article
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3 authors.
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Abstract
Polygalacturonases represents an important member of pectinases group of enzymes with diverse industrial applications and is widely distributed among fungi, bacteria, yeasts, plants and some plant parasitic nematodes. An endo-polygalacturonase from a new fungal source Aspergillus fumigatus MTCC 2584 was produced under solid-state fermentation conditions and was purified simply by acetone precipitation and gel-filtration chromatography technique. The approximate molecular weight of the purified PG was found to be 43.0 kDa as revealed by SDS-PAGE. The pH optimum of the purified enzyme was found to be 10.0 and was stable in the pH range of 7-10. The optimum temperature of purified PG was found to be 30 °C. The Km and Kcat of the purified enzyme were 2.4 mg/ml and 44 s
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