Article3 Biotech2017
Purification, characterization and retting of Crotolaria juncea fibres by an alkaline pectin lyase from Fusarium oxysporum MTCC 1755.
Article in 3 Biotech, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 20 citations in OpenAlex.
- Fungal pectinases: an insight into production, innovations and applications.World journal of microbiology & biotechnology · 2023Review
- Heterologous Expression and Characterization of a Novel Exo-Polygalacturonase fromJournal of microbiology and biotechnology · 2023Article
- Flow-cytometric cell sorting coupled with UV mutagenesis for improving pectin lyase expression.Frontiers in bioengineering and biotechnology · 2023Article
- Genome mining of3 Biotech · 2022Article
- Green Degumming Technology of Hemp and a Comparison between Chemical and Biological Degumming.ACS omega · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using solid-state fermentation, production of an industrially important pectin lyase from a fungal strain Fusarium oxysporum MTCC 1755 was attempted, which was further subjected to purification and characterization. The enzyme was purified by three steps, namely ammonium sulfate fractionation, cation-exchange chromatography on CM cellulose followed by gel filtration chromatography using Sephadex G-100 column. A 16-fold purification with 31.2% yield and 3.2 U/mg specific activity was achieved. The optimum pH of the purified enzyme was 9.0 and stability ranged from pH 5.0-7.0 for 24 h. Optimum temperature of purified enzyme was found to be 40 °C while temperature stability ranged from 10 to 50 °C for 30 min. The K
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Registered trials
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