2015
DOI: 10.1016/j.bbrc.2014.11.115
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Extracellular and cell-associated forms of Gluconobacter oxydans dextran dextrinase change their localization depending on the cell growth

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Cited by 18 publications
(16 citation statements)
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“…TtCITase-C showed homology with DDase belonging to GH family 15 and showed strong α-1,6 glucosyltransferase activity, similar to DDase from G. oxydans [26] and α-glucosidase from A. niger [2]. DDase produced dextran as the main product and a small amount of IMOs, while A. niger α-glucosidase produced IMOs with low DPs (2)(3)(4)(5)(6). However, in the present study, we did not detect the production of dextran or other high-DP products.…”
Section: Analysis Of Reaction Productsmentioning
confidence: 90%
See 1 more Smart Citation
“…TtCITase-C showed homology with DDase belonging to GH family 15 and showed strong α-1,6 glucosyltransferase activity, similar to DDase from G. oxydans [26] and α-glucosidase from A. niger [2]. DDase produced dextran as the main product and a small amount of IMOs, while A. niger α-glucosidase produced IMOs with low DPs (2)(3)(4)(5)(6). However, in the present study, we did not detect the production of dextran or other high-DP products.…”
Section: Analysis Of Reaction Productsmentioning
confidence: 90%
“…Commercialized IMOs with a degree of polarization (DP) ranging from 2 to 6 and lower numbers of α-1,6glucosidic linkages were produced from corn starch by αamylase and transglucosidase enzymes [3]. Dextranase has also been used to synthesize pure IMOs via the hydrolysis of dextran with α-1,6-glucan linkages, and longer IMOs with DP2-DP10 can be produced from sucrose-only substrates through the combined enzymatic action of dextranase and dextransucrase [4]. Furthermore, dextran dextrinase (DDase), belonging to the glycoside hydrolase (GH) family 15 isolated from Gluconobacter oxydans, was able to produce dextran with a high DP by the successive transfer of α-1,6-glucosyl units from maltodextrins [5].…”
Section: Introductionmentioning
confidence: 99%
“…However, it was previously unclear whether these two forms of the enzyme were in fact the same enzyme, and whether the strain is stimulated to simply secrete the intracellular dextran dextrinase when hydrolyzed starch and maltodextrins are present in the environment (Naessens et al, 2005). Recently, both forms of the enzyme were indeed shown to be identical (Sadahiro, Mori, Saburi, Okuyama, & Kimura, 2015). Compared to commercial dextran of a similar molecular mass produced by Leuconostoc mesenteroides, dextran produced by G. oxydans has a higher degree of branching and displays lower viscosity.…”
Section: Dextranmentioning
confidence: 99%
“…Some strains of Gluconobacter oxydans are known to produce an intracellular enzyme named dextran dextrinase (DDase, EC 2.4.1.2) catalyzing the synthesis of dextran using maltodextrins as substrate. DDase is able to transfer the non-reducing terminal glucosyl residues of maltodextrins to an acceptor substrate forming consecutive (a1!6) linkages (Naessens et al 2005;Sadahiro et al 2015). As a result of this activity a dextran polymer is produced, which contains some (a1!4) branches and (a1!4) linkages in (a1!6) glucosyl linear chains (Yamamoto, Yoshikawa, and Okada 1993).…”
Section: Dextran Dextrinasesmentioning
confidence: 99%