ArticleMicrobial cell factories2006
Revisiting the Cellulosimicrobium cellulans yeast-lytic beta-1,3-glucanases toolbox: a review.
Article in Microbial cell factories, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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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Who cites it
23 citing papers in PubMed, 73 citations in OpenAlex.
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- Novel, cold-adapted D-laminaribiose- and D-glucose-releasing GH16 endo-β-1,3-glucanase fromFrontiers in microbiology · 2024Article
- A First Expression, Purification and Characterization of Endo-β-1,3-Glucanase fromJournal of fungi (Basel, Switzerland) · 2023Article
- A Rapid and Efficient Method for the Extraction of Histone Proteins.Journal of proteome research · 2023Article
- Isolation, Screening, and Degradation Characteristics of a Quinclorac-Degrading Bacterium, Strain D, and Its Potential for Bioremediation of Rice Fields Polluted by Quinclorac.Microbiology spectrum · 2021Article
- Cellulosimicrobium fucosivorans sp. nov., isolated from San Elijo Lagoon, contains a fucose metabolic pathway linked to carotenoid production.Archives of microbiology · 2021Article
- Novel Anti-Fungal d-Laminaripentaose-Releasing Endo-β-1,3-glucanase with a RICIN-like Domain fromBiomolecules · 2021Article
- Analysis and application of a suite of recombinant endo-β(1,3)-D-glucanases for studying fungal cell walls.Microbial cell factories · 2021Article
- Enhancement of β-Glucan Biological Activity Using a Modified Acid-Base Extraction Method fromMolecules (Basel, Switzerland) · 2021Article
- A case report of the differential diagnosis of Cellulosimicrobium cellulans-infected endocarditis combined with intracranial infection by conventional blood culture and second-generation sequencing.BMC infectious diseases · 2020Article
- Effects of Different Carbon Sources on Enzyme Production and Ultrastructure of Cellulosimicrobium cellulans.Current microbiology · 2019Article
- The Interior Surfaces of Wooden Barrels Are an Additional Microbial Inoculation Source for Lambic Beer Production.Applied and environmental microbiology · 2019Article
- Isolation of β-1,3-Glucanase-Producing Microorganisms fromMolecules (Basel, Switzerland) · 2018Article
- Wort Substrate Consumption and Metabolite Production During Lambic Beer Fermentation and Maturation Explain the Successive Growth of Specific Bacterial and Yeast Species.Frontiers in microbiology · 2018Article
- Functional and structural properties of a novel cellulosome-like multienzyme complex: efficient glycoside hydrolysis of water-insoluble 7-xylosyl-10-deacetylpaclitaxel.Scientific reports · 2015Article
- Bioflocculant production from untreated corn stover using Cellulosimicrobium cellulans L804 isolate and its application to harvesting microalgae.Biotechnology for biofuels · 2015Article
- Draft Genome Sequence of Cellulosimicrobium sp. Strain MM, Isolated from Arsenic-Rich Microbial Mats of a Himalayan Hot Spring.Genome announcements · 2014Article
- Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatus.Folia microbiologica · 2014Article
- β-1,3-glucan modifying enzymes in Aspergillus fumigatus.Frontiers in microbiology · 2013Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulosimicrobium cellulans (also known with the synonyms Cellulomonas cellulans, Oerskovia xanthineolytica, and Arthrobacter luteus) is an actinomycete that excretes yeast cell wall lytic enzyme complexes containing endo-beta-1,3-glucanases [EC 3.2.1.39 and 3.2.1.6] as key constituents. Three genes encoding endo-beta-1,3-glucanases from two C. cellulans strains have been cloned and characterised over the past years. The betaglII and betaglIIA genes from strain DSM 10297 (also known as O. xanthineolytica LL G109) encoded proteins of 40.8 and 28.6 kDa, respectively, whereas the beta-1,3-glucanase gene from strain ATCC 21606 (also known as A. luteus 73-14) encoded a 54.5 kDa protein. Alignment of their deduced amino acid sequences reveal that betaglII and betaglIIA have catalytic domains assigned to family 16 of glycosyl hydrolases, whereas the catalytic domain from the 54.5 kDa glucanase belongs to family 64. Notably, both betaglII and the 54.5 kDa beta-1,3-glucanase are multidomain proteins, having a lectin-like C-terminal domain that has been assigned to family 13 of carbohydrate binding modules, and that confers to beta-1,3-glucanases the ability to lyse viable yeast cells. Furthermore, betaglII may also undergo posttranslational proteolytic processing of its C-terminal domain, resulting in a truncated enzyme retaining its glucanase activity but with very low yeast-lytic activity. In this review, the diversity in terms of structural and functional characteristics of the C. cellulans beta-1,3-glucanases has been compiled and compared.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.