DEMONSTRATION OF CURDLAN-TYPE POLYSACCHARIDE AND SOME OTHER Β-1, 3-Glucan IN MICROORGANISMS WITH ANILINE BLUE

Nakanishi, Itaru; Kimura, Kazutsugu; Suzuki, Takashi; Ishikawa, M.; Banno, Isao; Sakane, Takeshi; Harada, Tokuya

doi:10.2323/jgam.22.1

Cited by 92 publications

(36 citation statements)

References 2 publications

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“…The KOH solubilization test was done according to an accepted method (Gregersen, 1978). Curdlan-type polysaccharide was detected using aniline blue dye (Wako) and an appropriate staining method (Nakanishi et al, 1976). Hydrolysis of neutral and alkaline pectate gels was determined using previously described methods (Hildebrand, 1971).…”

Section: Methodsmentioning

confidence: 99%

Reclassification of ‘Pseudomonas fluorescens subsp. cellulosa’ NCIMB 10462 (Ueda et al. 1952) as Cellvibrio japonicus sp. nov. and revival of Cellvibrio vulgaris sp. nov., nom. rev. and Cellvibrio fulvus sp. nov., nom. rev.

Humphry

Black

Cummings

2003

International Journal of Systematic and Evolutionary Microbiology

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Section: Methodsmentioning

confidence: 99%

Reclassification of ‘Pseudomonas fluorescens subsp. cellulosa’ NCIMB 10462 (Ueda et al. 1952) as Cellvibrio japonicus sp. nov. and revival of Cellvibrio vulgaris sp. nov., nom. rev. and Cellvibrio fulvus sp. nov., nom. rev.

Humphry

Black

Cummings

2003

International Journal of Systematic and Evolutionary Microbiology

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“…It was also noted that although the colonies on ABA remained white on prolonged incubation, flecks of blue staining appeared in areas of high bacterial density. These areas did not develop the dry pellicle typically associated with curdlan production (43), nor did they yield any blue-staining colonies that might have represented revertants to the Crd ϩ phenotype. The Agrobacterium gene disrupted in LTU121 encodes phosphatidylserine synthase and is essential for curdlan produc- a Biomass, curdlan production, and phospholipid content were estimated with 7-day ADB cultures.…”

Section: Origin Of the Phomentioning

confidence: 95%

Cloning and Characterization of the Phosphatidylserine Synthase Gene of Agrobacterium sp. Strain ATCC 31749 and Effect of Its Inactivation on Production of High-Molecular-Mass (1→3)-β- d -Glucan (Curdlan)

Karnezis¹,

Fisher²,

Neumann³

et al. 2002

J Bacteriol

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Genes involved in the production of the extracellular (133)-␤-glucan, curdlan, by Agrobacterium sp. strain ATCC 31749 were described previously (Stasinopoulos et al., Glycobiology 9:31-41, 1999). To identify additional curdlan-related genes whose protein products occur in the cell envelope, the transposon TnphoA was used as a specific genetic probe. One mutant was unable to produce high-molecular-mass curdlan when a previously uncharacterized gene, pss AG , encoding a 30-kDa, membrane-associated phosphatidylserine synthase was disrupted. The membranes of the mutant lacked phosphatidylethanolamine (PE), whereas the phosphatidylcholine (PC) content was unchanged and that of both phosphatidylglycerol and cardiolipin was increased. In the mutant, the continued appearance of PC revealed that its production by this Agrobacterium strain is not solely dependent on PE in a pathway controlled by the Pss AG protein at its first step. Moreover, PC can be produced in a medium lacking choline. When the pss AG ::TnphoA mutation was complemented by the intact pss AG gene, both the curdlan deficiency and the phospholipid profile were restored to wild-type, demonstrating a functional relationship between these two characteristics. The effect of the changed phospholipid profile could occur through an alteration in the overall charge distribution on the membrane or a specific requirement for PE for the folding into or maintenance of an active conformation of any or all of the structural proteins involved in curdlan production or transport.

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“…The culture was diluted 10-and 100-fold in a mixture of 50% seawater and 50% water. The undiluted and diluted cultures (10 l) were spread onto a 2% (wt/vol) agar plate containing 2SM and 0.005% (wt/vol) methyl blue as an indicator of 1,3-␤-glucan presence (21), and the plate was incubated at 28°C.…”

Section: Chemicals and Enzymes Laminarin P-nitrophenol (Pnp) P-nitmentioning

confidence: 99%

Discovery and Characterization of a Distinctive Exo-1,3/1,4-β-Glucanase from the Marine Bacterium Pseudoalteromonas sp. Strain BB1

Nakatani

Lamont

Cutfield

2010

Appl Environ Microbiol

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Marine bacteria residing on local red, green, and brown seaweeds were screened for exo-1,3-␤-glucanase (ExoP) activity. Of the 90 bacterial species isolated from 32 seaweeds, only one, a Pseudoalteromonas sp., was found to display such activity. It was isolated from a Durvillaea sp., a brown kelp known to contain significant amounts of the storage polysaccharide laminarin (1,3-␤-D-glucan with some 1,6-␤ branching). Four chromatographic steps were utilized to purify the enzyme (ExoP). Chymotryptic digestion provided peptide sequences for primer design and subsequent gene cloning. The exoP gene coded for 840 amino acids and was located just 50 bp downstream from a putative lichenase (endo-1,3-1,4-␤-glucanase) gene, suggesting possible cotranscription of these genes. Sequence comparisons revealed ExoP to be clustered within a group of bacterial glycosidases with high similarity to a group of glycoside hydrolase (GH3) plant enzymes, of which the barley exo-1,3/1,4-␤-glucanase (ExoI) is the best characterized. The major difference between the bacterial and plant proteins is an extra 200-to 220-amino-acid extension at the C terminus of the former. This additional sequence does not correlate with any known functional domain, but ExoP was not active against laminarin when this region was removed. Production of recombinant ExoP allowed substrate specificity studies to be performed. The enzyme was found to possess similar levels of exoglucanase activity against both 1,4-␤ linkages and 1,3-␤ linkages, and so ExoP is designated an exo-1,3/1,4-␤-exoglucanase, the first such bacterial enzyme to be characterized. This broader specificity could allow the enzyme to assist in digesting both cell wall cellulose and cytoplasmic laminarin.

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DEMONSTRATION OF CURDLAN-TYPE POLYSACCHARIDE AND SOME OTHER Β-1, 3-Glucan IN MICROORGANISMS WITH ANILINE BLUE

Cited by 92 publications

References 2 publications

Reclassification of ‘Pseudomonas fluorescens subsp. cellulosa’ NCIMB 10462 (Ueda et al. 1952) as Cellvibrio japonicus sp. nov. and revival of Cellvibrio vulgaris sp. nov., nom. rev. and Cellvibrio fulvus sp. nov., nom. rev.

Reclassification of ‘Pseudomonas fluorescens subsp. cellulosa’ NCIMB 10462 (Ueda et al. 1952) as Cellvibrio japonicus sp. nov. and revival of Cellvibrio vulgaris sp. nov., nom. rev. and Cellvibrio fulvus sp. nov., nom. rev.

Cloning and Characterization of the Phosphatidylserine Synthase Gene of Agrobacterium sp. Strain ATCC 31749 and Effect of Its Inactivation on Production of High-Molecular-Mass (1→3)-β- d -Glucan (Curdlan)

Discovery and Characterization of a Distinctive Exo-1,3/1,4-β-Glucanase from the Marine Bacterium Pseudoalteromonas sp. Strain BB1

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