Synthesis of oligo- and polysaccharides by Lactobacillus reuteri 121 reuteransucrase at high concentrations of sucrose

Meng, Xiangfeng; Dobruchowska, Justyna M.; Gerwig, Gerrit J.; Kamerling, Johannis P.; Dijkhuizen, Lubbert

doi:10.1016/j.carres.2015.07.011

Cited by 19 publications

(11 citation statements)

References 25 publications

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“…The polysaccharide synthesized by GTFA was also found to reach its maximum size in a relatively short time, with the simultaneous detection of oligosaccharides [ 84 ]. The reuteran polysaccharide size did not increase further, not even with the availability of excess sucrose [ 87 ]. The detection of HMM polysaccharide with a maximum size indicates a processive mode, while the detection of oligosaccharides points at non-processive mode.…”

Section: Mechanism Of α-Glucan Synthesis By Family Gh70 Gs Enzymesmentioning

confidence: 99%

“…The ratio of oligosaccharide synthesis versus polysaccharide synthesis of GTFA from L. reuteri 121 is directly proportional to the concentration of sucrose. However, the sizes of the polysaccharides produced at different sucrose concentrations were identical [ 87 ]. At present, it remains unknown what determines the molecular size of the α-glucan polysaccharides synthesized by GS enzymes.…”

Section: Mechanism Of α-Glucan Synthesis By Family Gh70 Gs Enzymesmentioning

confidence: 99%

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Structure–function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes

Meng

Gangoiti

Bai

et al. 2016

Cell. Mol. Life Sci.

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Lactic acid bacteria (LAB) are known to produce large amounts of α-glucan exopolysaccharides. Family GH70 glucansucrase (GS) enzymes catalyze the synthesis of these α-glucans from sucrose. The elucidation of the crystal structures of representative GS enzymes has advanced our understanding of their reaction mechanism, especially structural features determining their linkage specificity. In addition, with the increase of genome sequencing, more and more GS enzymes are identified and characterized. Together, such knowledge may promote the synthesis of α-glucans with desired structures and properties from sucrose. In the meantime, two new GH70 subfamilies (GTFB- and GTFC-like) have been identified as 4,6-α-glucanotransferases (4,6-α-GTs) that represent novel evolutionary intermediates between the family GH13 and “classical GH70 enzymes”. These enzymes are not active on sucrose; instead, they use (α1 → 4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize novel α-glucans by introducing linear chains of (α1 → 6) linkages. All these GH70 enzymes are very interesting biocatalysts and hold strong potential for applications in the food, medicine and cosmetic industries. In this review, we summarize the microbiological distribution and the structure–function relationships of family GH70 enzymes, introduce the two newly identified GH70 subfamilies, and discuss evolutionary relationships between family GH70 and GH13 enzymes.Electronic supplementary materialThe online version of this article (doi:10.1007/s00018-016-2245-7) contains supplementary material, which is available to authorized users.

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Section: Mechanism Of α-Glucan Synthesis By Family Gh70 Gs Enzymesmentioning

confidence: 99%

Section: Mechanism Of α-Glucan Synthesis By Family Gh70 Gs Enzymesmentioning

confidence: 99%

Structure–function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes

Meng

Gangoiti

Bai

et al. 2016

Cell. Mol. Life Sci.

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“…Hetero-EPS consist of more than one carbohydrate moiety, and generally are synthesized intracellularly from activated sugars . LAB homo-EPS consist of a single type of monosaccharide, generally d -glucose or d -fructose, and can be divided into α-glucans (e.g., dextran, mutan, alternan, and reuteran) and β-fructans (e.g., inulin and levan). − Most LAB homo-EPS known are produced from sucrose by extracellular glucansucrase and fructansucrase enzymes. ,, Lactobacillus reuteri 121 uses the GtfA glucansucrase to convert sucrose into an α-glucan (reuteran) with both α1→4 and α1→6 linkages, mostly alternating. − Glucansucrases are glycoside hydrolase enzymes belonging to family GH70 as classified by Carbohydrate Active Enzyme Database ().…”

Section: Introductionmentioning

confidence: 99%

Lactobacillus reuteri Strains Convert Starch and Maltodextrins into Homoexopolysaccharides Using an Extracellular and Cell-Associated 4,6-α-Glucanotransferase

Bai

Böger

Kaaij

et al. 2016

J. Agric. Food Chem.

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Exopolysaccharides (EPS) of lactic acid bacteria (LAB) are of interest for food applications. LAB are well-known to produce α-glucan from sucrose by extracellular glucansucrases. Various Lactobacillus reuteri strains also possess 4,6-α-glucanotransferase (4,6-α-GTase) enzymes. Purified 4,6-α-GTases (e.g., GtfB) were shown to act on starches (hydrolysates), cleaving α1→4 linkages and synthesizing α1→6 linkages, yielding isomalto-/maltopolysaccharides (IMMP). Here we report that also L. reuteri cells with these extracellular, cell-associated 4,6-α-GTases synthesize EPS (α-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by L. reuteri 121 cells showed that these have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. Various IMMP-like EPS are efficiently used as growth substrates by probiotic Bifidobacterium strains that possess amylopullulanase activity. IMMP-like EPS thus have potential prebiotic activity and may contribute to the application of probiotic L. reuteri strains grown on maltodextrins or starches as synbiotics.

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“…This approach permitted the preparation of amylose with narrow MW distribution, amylose hybrids, and amylose-functionalized materials [ 186 ]. Linear and branched oligosaccharides with mixed α(1–3) and α(1–4) linkages were synthesized using a glucansucrase from Lactobacillus reuteri [ 187 – 188 ].…”

Section: Reviewmentioning

confidence: 99%

Progress and challenges in the synthesis of sequence controlled polysaccharides

Fittolani¹,

Tyrikos‐Ergas²,

Vargová³

et al. 2021

Beilstein J. Org. Chem.

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The sequence, length and substitution of a polysaccharide influence its physical and biological properties. Thus, sequence controlled polysaccharides are important targets to establish structure–properties correlations. Polymerization techniques and enzymatic methods have been optimized to obtain samples with well-defined substitution patterns and narrow molecular weight distribution. Chemical synthesis has granted access to polysaccharides with full control over the length. Here, we review the progress towards the synthesis of well-defined polysaccharides. For each class of polysaccharides, we discuss the available synthetic approaches and their current limitations.

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Synthesis of oligo- and polysaccharides by Lactobacillus reuteri 121 reuteransucrase at high concentrations of sucrose

Cited by 19 publications

References 25 publications

Structure–function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes

Structure–function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes

Lactobacillus reuteri Strains Convert Starch and Maltodextrins into Homoexopolysaccharides Using an Extracellular and Cell-Associated 4,6-α-Glucanotransferase

Progress and challenges in the synthesis of sequence controlled polysaccharides

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