ArticleJournal of microbiology (Seoul, Korea)2013
Biochemical characterization of chitinase 2 expressed during the autolytic phase of the inky cap, Coprinellus congregatus.
Article in Journal of microbiology (Seoul, Korea), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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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
6 citing papers in PubMed, 21 citations in OpenAlex.
- Novel Chitin Deacetylase fromMetabolites · 2023Article
- Chitinase Is Involved in the Fruiting Body Development of Medicinal FungusLife (Basel, Switzerland) · 2023Article
- Transcriptome analysis of genes associated with autolysis of Coprinus comatus.Scientific reports · 2022Article
- Identification and characterization of a marine-derived chitinolytic fungus, Acremonium sp. YS2-2.Journal of microbiology (Seoul, Korea) · 2019Article
- Lentinula edodes Genome Survey and Postharvest Transcriptome Analysis.Applied and environmental microbiology · 2017Article
- Antifungal chitinase against human pathogenic yeasts from Coprinellus congregatus.Journal of microbiology (Seoul, Korea) · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungal cell walls consist of various glucans and chitin. The inky cap, Coprinellus congregatus, produces mushrooms at 25°C in a regime of 15 h light/9 h dark, and then the mushroom is autolyzed rapidly to generate black liquid droplets in which no cell walls are detected by microscopy. Chitinase cDNA from the mature mushroom tissues of C. congregatus, which consisted of 1,622 nucleotides (chi2), was successfully cloned using the rapid amplification of cDNA ends polymerase chain reaction technique. The deduced 498 amino acid sequence of Chi2 had a conserved catalytic domain as in other fungal chitinase family 18 enzymes. The Chi2 enzyme was purified from the Pichia pastoris expression system, and its estimated molecular weight was 68 kDa. The optimum pH and temperature of Chi2 was pH 4.0 and 35°C, respectively when 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside was used as the substrate. The K m value and V max for the substrate A, 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, was 0.175 mM and 0.16 OD min(-1)unit(-1), respectively.
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