Subcellular Localization of D-Glucanases in Bacteroides oralis Ig4a

Takahashi, Nobuhiro; Satoh, Y.; Takamori, Kenshiro

doi:10.1099/00221287-131-5-1077

Cited by 10 publications

(13 citation statements)

References 18 publications

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“…The intracellular dextranase, D 4, was very similar to D 1 in molecular weight, pH, and temperature optima as well as mode of action (Table 1). Dextranase activity has also been detected in both intra-and extracellular fractions of Bacteroides oralis Ig4a obtained from human dental plaque (205) (Table 1).…”

Section: Endodextranases From Bacteriamentioning

confidence: 96%

“…Most of the bacterial dextranase producers have the ability to synthesize several ␣-glucosidases with different subcellular localizations and substrate specificities simultaneously (29,30,205). Two extracellular dextranases (D 1 and D 2 ) and one intracellular dextranase (D 4 ) from Pseudomonas sp.…”

Section: Endodextranases From Bacteriamentioning

confidence: 99%

“…A wide range of bacterial species, such as Bacteroides spp., Bifidobacterium spp., and Fusobacterium spp. associated with dental plaque, produce inducible dextran-hydrolyzing enzymes (26,76,86,196,205).…”

Section: Role Of Dextranases In Non-dextran-producing Microorganismsmentioning

confidence: 99%

See 2 more Smart Citations

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Khalikova

Susi

Korpela

2005

Microbiol Mol Biol Rev

228

152

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Dextran is a chemically and physically complex polymer, breakdown of which is carried out by a variety of endo- and exodextranases. Enzymes in many groups can be classified as dextranases according to function: such enzymes include dextranhydrolases, glucodextranases, exoisomaltohydrolases, exoisomaltotriohydrases, and branched-dextran exo-1,2-α-glucosidases. Cycloisomalto-oligosaccharide glucanotransferase does not formally belong to the dextranases even though its side reaction produces hydrolyzed dextrans. A new classification system for glycosylhydrolases and glycosyltransferases, which is based on amino acid sequence similarities, divides the dextranases into five families. However, this classification is still incomplete since sequence information is missing for many of the enzymes that have been biochemically characterized as dextranases. Dextran-degrading enzymes have been isolated from a wide range of microorganisms. The major characteristics of these enzymes, the methods for analyzing their activities and biological roles, analysis of primary sequence data, and three-dimensional structures of dextranases have been dealt with in this review. Dextranases are promising for future use in various scientific and biotechnological applications

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Section: Endodextranases From Bacteriamentioning

confidence: 96%

Section: Endodextranases From Bacteriamentioning

confidence: 99%

See 1 more Smart Citation

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Khalikova

Susi

Korpela

2005

Microbiol Mol Biol Rev

228

152

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“…RM1 enzyme. Many bacterial -1,3-glucanases, such as those of Flavobacterium sp., 15) Pseudomonas sp., 18) Streptomyces chartreuses, 19) Bacteroides oralis, 20,21) and Bacillus circulans, 22) have been studied from the same point of view as that for the Bacillus sp. RM1 enzyme to remove tooth plaque created by oral bacteria, but the gene of these enzymes has not been cloned, except for that of the Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

“…RM1 -1,3-glucanase was named as mutanase (EC.3.2.1.59) that hydrolyzes mutan formed by an oral bacterium, Streptococcus mutans. The presence of mutanases has been also reported in several bacteria [14][15][16][17][18][19][20][21][22] and filamentous fungi. [23][24][25][26][27][28][29][30][31][32][33] Among these -1,3-glucanases, the genes of y To whom correspondence should be addressed.…”

mentioning

confidence: 98%

Cloning and Expression of an α-1,3-Glucanase Gene fromBacillus circulansKA-304: The Enzyme Participates in Protoplast Formation ofSchizophyllum commune

Yano

Wakayama

Tachiki

2006

Bioscience, Biotechnology, and Biochemistry

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Isolation of dextran‐hydrolyzing intestinal bacteria and characterization of their dextranolytic activities

et al. 2015

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The aim of this study was to isolate dextran-hydrolyzing bacteria from the human intestines and to identify their dextranolytic enzymes. For this, dextranase-producing microorganisms were screened from fecal samples by using blue dextran-containing media. Colonies producing a decolorized zone were isolated and they were grouped using RAPD-PCR. 16S rRNA gene sequencing analysis revealed the isolates were Bacteroides (B.) thetaiotaomicron, B. ovatus, B. vulgatus, B. dorei, B. xylanisolvens, B. uniformis, and Veillonella (V.) rogosae. Thin layer chromatography analysis showed that the dextranases exhibit mainly endo-type activity and produce various oligosaccharides including isomaltose and isomaltotriose. Zymogram analysis demonstrated that enzymes localized mainly in the cell membrane fraction and the molecular weight was 50-70 kDa. When cultured in a dextran-containing medium, all strains isolated in this study produced short-chain fatty acids, with butyric acid as the major compound. This is the first study to report that human intestinal B. xylanisolvens, B. dorei, and V. rogosae metabolize dextran utilizing dextranolytic enzymes.

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Subcellular Localization of D-Glucanases in Bacteroides oralis Ig4a

Cited by 10 publications

References 18 publications

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Cloning and Expression of an α-1,3-Glucanase Gene fromBacillus circulansKA-304: The Enzyme Participates in Protoplast Formation ofSchizophyllum commune

Isolation of dextran‐hydrolyzing intestinal bacteria and characterization of their dextranolytic activities

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