A glycoside hydrolase family 31 dextranase with high transglucosylation activity from <i>Flavobacterium johnsoniae</i>

Gozu, Yoshifumi; Ishizaki, Yuichi; Hosoyama, Yuhei; Miyazaki, Takatsugu; Nishikawa, Atsushi; Tonozuka, Takashi

doi:10.1080/09168451.2016.1182852

Cited by 20 publications

(22 citation statements)

References 44 publications

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“…On the other hand, no direct Figure reproduced from Ref. [16] hydrogen bond is seen between Glc À3 and FjDex31A.…”

Section: N-terminalmentioning

confidence: 92%

“…Dextranase (α‐1,6‐glucan‐6‐glucanohydrolase; EC 3.2.1.11) hydrolyzes the α‐1,6‐glucosidic linkages of dextran in an endo‐acting manner. Previously, all endo‐acting dextranases identified belonged to the GH49 or GH66 families , but we presented the first report of a dextranase belonging to GH31 from Flavobacterium johnsoniae . The whole genome of this Gram‐negative bacterium has already been sequenced , and a GH31 enzyme encoded in the genome of F. johnsoniae , Fjoh_4430, hydrolyzes dextran to produce a mixture of isomaltooligosaccharides .…”

Section: Introductionmentioning

confidence: 99%

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Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31

et al. 2019

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Glycoside hydrolase family (GH) 31 contains a large variety of enzymes, but the major members are enzymes that act on relatively small oligosaccharides such as α‐glucosidase. Here, we determined the crystal structure of Flavobacterium johnsoniae dextranase (FjDex31A), an enzyme from F. johnsoniae that hydrolyzes a polysaccharide, dextran. FjDex31A is composed of four domains: an N‐terminal domain, a catalytic domain, a proximal C‐terminal domain, and a distal C‐terminal domain, as observed in typical GH31 enzymes. However, the architecture of active site residues in FjDex31A, other than subsite −1, is markedly different from that of other GH31 enzymes. The FjDex31A structure in complex with isomaltotriose shows that Gly273 and Tyr524, both of which interact with an α‐glucose residue at subsite −2, as well as Trp376 and Leu308‐cisGln309, are especially unique to FjDex31A. Site‐directed mutagenesis of Gly273 and Tyr524 resulted in a decrease in the hydrolysis of polysaccharides dextran and pullulan, as well as that of the disaccharide isomaltose. These results suggest that, regardless of the length of sugar chains of the substrates, binding of FjDex31A to the substrates at subsite −2 is likely to be important for its activity. Database Structural data are available in the Protein Data Bank under the accession numbers http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6JR6, http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6JR7, and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6JR8.

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“…On the other hand, no direct Figure reproduced from Ref. [16] hydrogen bond is seen between Glc À3 and FjDex31A.…”

Section: N-terminalmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31

et al. 2019

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“…P. hydrogenivorans is a psychrotolerant bacterium able to utilize a variety of organic acids, alcohols, and some simple sugars (Sizova and Panikov 2007). Also, F. johnsoniae can utilize polysaccharides such as chitin and has glycoside hydroxylase family 31 enzymes, which exhibit various substrate specificities (Gozu et al 2016; Larsbrink et al 2016). In contrast, a small amount of rice bran was degraded at a 5 h HRT (TOC concentrations were very low [<10 mg l −1 , Fig.…”

Section: Discussionmentioning

confidence: 99%

Hydraulic retention time and pH affect the performance and microbial communities of passive bioreactors for treatment of acid mine drainage

et al. 2017

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For acceleration of removing toxic metals from acid mine drainage (AMD), the effects of hydraulic retention time (HRT) and pH on the reactor performance and microbial community structure in the depth direction of a laboratory-scale packed-bed bioreactor containing rice bran as waste organic material were investigated. The HRT was shortened stepwise from 25 to 12 h, 8 h, and 6 to 5 h under the neutral condition using AMD neutralized with limestone (pH 6.3), and from 25 to 20 h, 12 h, and 8 to 7 h under the acid condition using AMD (pH 3.0). Under the neutral condition, the bioreactor stably operated up to 6 h HRT, which was shorter than under the acid condition (up to 20 h HRT). During stable sulfate reduction, both the organic matter-remaining condition and the low oxidation–reduction potential condition in lower parts of the reactor were observed. Principal coordinate analysis of Illumina sequencing data of 16S rRNA genes revealed a dynamic transition of the microbial communities at the boundary between stable and unstable operation in response to reductions in HRT. During stable operation under both the neutral and acid conditions, several fermentative operational taxonomic units (OTUs) from the phyla Firmicutes and Bacteroidetes dominated in lower parts of the bioreactor, suggesting that co-existence of these OTUs might lead to metabolic activation of sulfate-reducing bacteria. In contrast, during unstable operation at shorter HRTs, an OTU from the candidate phylum OP11 were found under both conditions. This study demonstrated that these microorganisms can be used to monitor the treatment of AMD, which suggests stable or deteriorated performance of the system.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0440-z) contains supplementary material, which is available to authorized users.

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“…According to classifications of the glycoside hydrolase family (GH), GH49, GH31, and GH66 groups include dextranases [1]. The GH49 is a group of an inverting dextranases, whereas exo-type αglucosidases predominate in the GH31 group and the recently discovered endo-type dextranase [2] is a unique member in this family. The GH66 group includes the dextran- (CIs) using an intramolecular transglycosylation mechanism [3].…”

Section: Introductionmentioning

confidence: 99%

Engineered dextranase from Streptococcus mutans enhances the production of longer isomaltooligosaccharides

Klahan

Okuyama

Jinnai

et al. 2018

Bioscience, Biotechnology, and Biochemistry

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Herein, we investigated enzymatic properties and reaction specificities of Streptococcus mutans dextranase, which hydrolyzes α-(1→6)-glucosidic linkages in dextran to produce isomaltooligosaccharides. Reaction specificities of wild-type dextranase and its mutant derivatives were examined using dextran and a series of enzymatically prepared p-nitrophenyl α-isomaltooligosaccharides. In experiments with 4-mg·mL dextran, isomaltooligosaccharides with degrees of polymerization (DP) of 3 and 4 were present at the beginning of the reaction, and glucose and isomaltose were produced by the end of the reaction. Increased concentrations of the substrate dextran (40 mg·mL) yielded isomaltooligosaccharides with higher DP, and the mutations T558H, W279A/T563N, and W279F/T563N at the -3 and -4 subsites affected hydrolytic activities of the enzyme, likely reflecting decreases in substrate affinity at the -4 subsite. In particular, T558H increased the proportion of isomaltooligosaccharide with DP of 5 in hydrolysates following reactions with 4-mg·mL dextran.Abbreviations CI: cycloisomaltooligosaccharide; CITase: CI glucanotransferase; CITase-Bc: CITase from Bacillus circulans T-3040; DP: degree of polymerization of glucose unit; GH: glycoside hydrolase family; GTF: glucansucrase; HPAEC-PAD: high performance anion-exchange chromatography-pulsed amperometric detection; IG: isomaltooligosaccharide; IGn: IG with DP of n (n, 2‒5); PNP: p-nitrophenol; PNP-Glc: p-nitrophenyl α-glucoside; PNP-IG: p-nitrophenyl isomaltooligosaccharide; PNP-IGn: PNP-IG with DP of n (n, 2‒6); SmDex: dextranase from Streptococcus mutans; SmDexTM: S. mutans ATCC25175 SmDex bearing Gln100‒Ile732.

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A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae

Cited by 20 publications

References 44 publications

Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31

Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31

Hydraulic retention time and pH affect the performance and microbial communities of passive bioreactors for treatment of acid mine drainage

Engineered dextranase from Streptococcus mutans enhances the production of longer isomaltooligosaccharides

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