ArticleCurrent microbiology2022
Production, Partial Purification, and Characterization of Polygalacturonase from Aureobasidium pullulans P56 under Submerged Fermentation Using Agro-Industrial Wastes.
Article in Current microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 9 citations in OpenAlex.
- Food Biotechnology Potential of Grape-DerivedFoods (Basel, Switzerland) · 2026Article
- Computational Design of a Thermo-Acidostable Endo-Polygalacturonase for Efficient Juice Extraction.Foods (Basel, Switzerland) · 2026Article
- Functionality Enhancement of Pullulan-Based Composites for Food Packaging Applications.Comprehensive reviews in food science and food safety · 2026Review
- Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations.Food science & nutrition · 2025Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Polygalacturonase (PGase) production by Aureobasidium pullulans P56 under submerged fermentation was investigated using agro-industrial wastes and commercial carbon and nitrogen sources. The maximum PGase concentration was equivalent to 8.6 U/mL that was obtained in presence of citrus pectin at 150 rpm, 30 °C, pH = 5.5, and 60 h of fermentation conditions. However, a significant amount of enzyme production was also recorded upon the utilization of corncob (5.3 U/mL) and wheat bran (4.4 U/mL) as carbon sources. Amongst the different nitrogen sources, the highest enzyme production (8.2 U/mL) was obtained in presence of ammonium sulphate and yeast extract simultaneously at a ratio of 1:1. The enzyme was partially purified by gel filtration using Sephadex G50 equilibrated and washed with 50 mM-sodium acetate buffer. The obtained yield and specific activity were determined equivalent to 17% and 9.53 U/mg, respectively. The molecular weight of the partially purified enzyme was estimated as 54 kDa on SDS-PAGE. The conditions affecting the enzyme activity were determined and the highest enzyme activity was recorded at 40 °C and 4.5 pH. Amongst the tested metal ions, 2 and 5 mM of CaCl
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Registered trials
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