ArticleIndian journal of microbiology2012
Production, Purification of Exo-Polygalacturonase from Soil Isolate Paecilomyces variotii NFCCI 1769 and Its Application.
Article in Indian journal of microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 30 citations in OpenAlex.
- Development of a CRISPR/Cas9 RNP-mediated genetic engineering system in Paecilomyces variotii.Journal of microbiology (Seoul, Korea) · 2025Article
- Fungal pectinases: an insight into production, innovations and applications.World journal of microbiology & biotechnology · 2023Review
- Article
- Genomic and Genetic Insights Into a Cosmopolitan Fungus,Frontiers in microbiology · 2018Article
- Article
- Enhanced production of pectinase by Aspergillus terreus NCFT 4269.10 using banana peels as substrate.3 Biotech · 2016Article
- Preliminary Extraction and Identification of the 44.5 kDa Outer Membrane Proteins Isolated from Bovine Fusobacterium necrophorum (AB).Indian journal of microbiology · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of the present study was to produce exo-polygalacturonase from potent soil isolate by submerged fermentation and its application for fruit juice treatment. Pectinase producing strains were selectively isolated from pectin industry waste. A selected isolate C2 was found to produce significant amount of exo-polygalacturonase. The isolate was identified as Paecilomyces variotii on the basis of morphological characteristics and 18S rRNA gene sequence analysis. The exo-polygalacturonase produced by the isolate was purified by ammonium sulphate precipitation, size exclusion chromatography and ion exchange chromatography. The purified enzyme had MW of 39.4 kD based on SDS PAGE. Under partially optimized conditions, purified exo-polygalacturonase showed specific activity of 98.49 U/mg protein at pH 6.0 and 30°C. The enzyme was comparatively stable from 10 to 30°C and the activity decreased with increasing temperature. Purified enzyme brought about considerable reduction in viscosity of fruit juice samples.
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