4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H

Gangoiti, Joana; Leeuwen, Sander S. van; Gerwig, Gerrit J.; Duboux, Stéphane; Vafiadi, Christina; Pijning, Tjaard; Dijkhuizen, Lubbert

doi:10.1038/srep39761

Cited by 49 publications

(81 citation statements)

References 61 publications

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“…In GH70, four sub- groups of enzymes with distinct enzyme characteristics, i.e., the GS subgroup, the BrS subgroup, and the GTFB-like and GTFC-like subgroups of 4,6-␣-GTs, have been identified so far. According to Gangoiti et al, the 4,6-␣-GT subgroup was formed in the process of the evolution of ancient GH13 enzymes into GSs (19,40), and the BrS enzymes emerged after the separation of 4,6-␣-GTs, as demonstrated in the previous study (7).…”

Section: Evolutionary Intermediate Between Brs and Gs Enzymesmentioning

confidence: 77%

Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes

Yan

Wang

Xu³

et al. 2018

Appl Environ Microbiol

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Glucansucrases (GSs) in glycoside hydrolase family 70 (GH70) catalyze the synthesis of α-glucans from sucrose, a reaction that is widely seen in lactic acid bacteria (LAB). These enzymes have been implicated in many aspects of microbial life. Products of GSs have great commercial value as food supplements and medical materials; therefore, these enzymes have attracted much attention from both science and industry. Certain issues concerning the origin and evolution of GSs are still to be addressed, although an increasing number of GH70 enzymes have been characterized. This study describes a GS enzyme with the appearance of a branching sucrase (BrS). Structural analysis indicated that this GS enzyme produced a type of glucan composed of an α-(1→6) glucosidic backbone and α-(1→4) branches, as well as a considerable amount of α-(1→3) branches, distinguishing it from the GSs identified so far. Moreover, sequence-based analysis of the catalytic core of this enzyme suggested that it might be an evolutionary intermediate between the BrS and GS subgroups. These results provide an evolutionary link between these subgroups of GH70 enzymes and shed new light on the origination of GSs. GH70 GSs catalyze the synthesis of α-glucans from sucrose, a reaction that is widely seen in LAB. Products of these enzymes have great commercial value as food supplements and medical materials. Moreover, these enzymes have attracted much attention from scientists because they have potential in tailored synthesis of α-glucans with desired structures and properties. Although more and more GSs have been characterized, the origin and evolution of these enzymes have not been well addressed. This study describes a GS with the appearance of a BrS (i.e., high levels of similarity to BrSs in sequence analysis). Further analysis indicated that this enzyme synthesized a type of insoluble glucan composed of an α-(1→6) glucosidic backbone and many α-(1→4)- and α-(1→3)-linked branches, the linkage composition of which has rarely been reported in the literature. This BrS-like GS enzyme might be an evolutionary intermediate between BrS and GS enzymes.

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Section: Evolutionary Intermediate Between Brs and Gs Enzymesmentioning

confidence: 77%

Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes

Yan

Wang

Xu³

et al. 2018

Appl Environ Microbiol

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“…The glucansucrase was stable at temperatures up to 60 °C for at least 10 min in 20 mM Tris‐HCl buffer (pH 8.0) containing 1 mM CaCl 2 . They also reported an α‐4,3‐glucanotransferase from Lactobacillus fermentum NCC 2970, exhibiting greatest activity at pH 5.5 and 50 °C (Gangoiti, van Leeuwen et al., ). It converted amylose into a new type of polymer with alternating α‐1,3 and α‐1,4 bonds and α‐1,3,4 branch points.…”

Section: Specific Starch‐processing Enzymesmentioning

confidence: 96%

“…Glucansucrases are members of family GH70. Specific glucansucrases may be termed dextransucrases, mutansucrases, alternansucrases, reuteransucrases, α‐1,2‐branching dextransucrases, α‐4,6‐glucanotransferases, or α‐4,3‐glucanotransferases (Bai et al., ; Brison et al., ; Gangoiti, van Leeuwen et al., ; Gangoiti, Lamothe et al., ; Miao et al., ; Song et al., ). Gluansucrases are evolutionary intermediates between enzymes in the GH13 and GH70 families, but their substrate specificities are completely different (Kralj et al., ).…”

Section: Specific Starch‐processing Enzymesmentioning

confidence: 99%

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Miao

Jiang

Jin

et al. 2018

Comp Rev Food Sci Food Safe

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Starch is an abundant, natural, renewable resource, and present as the major storage carbohydrate in the seeds, roots, or tubers of many important food crops, such as maize, wheat, rice, potato, and cassava. Uses of native starches in most industrial applications are limited by their inherent properties. Hence, they are often structurally modified after isolation to enhance desirable attributes, to minimize undesirable attributes, or to create new attributes. Enzymatic, rather than chemical, approaches are used in the production of starch syrups, maltodextrins, and cyclodextrins. However, the desire for starch-active enzymes working optimally at high temperatures and low pH conditions with superior stability and activity is still not satisfied and this stimulates interest in developing novel and improved starch-active enzymes through a variety of strategies. This review provides current information on enzymes belonging to GH13, 57, 70, and 77 that can be used in structural modifications of the starch polysaccharides or to produce starch-derived products from them. The characteristics and catalytic mechanisms of microbial enzymes are discussed (including 4-α-glucanotransferase, branching enzyme, maltogenic amylase, cyclomaltodextrinase, amylosucrase, and glucansucrase). Product diversity after starch-converting reaction and utilization in industrial applications are also dealt with.

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“…Retaining transglucosylases, which catalyse polymerization reactions from non-nucleotide sugars, represent another category of glycan-synthesising enzymes that could be of interest in the production of block copolymers. Some α-transglucosylases, such as dextran dextrinases [16][17][18] [16][17][18][19] or α(1 → 3) (4,3-α-glucanotransferase) linkages can be formed. 19 Besides, the 4,6-α-GTase from Lactobacillus reuteri 121 has been used to produce isomalto/malto-polysaccharides (IMMPs) with a DP of up to 30.…”

Section: Introductionmentioning

confidence: 99%

“…Some α-transglucosylases, such as dextran dextrinases [16][17][18] [16][17][18][19] or α(1 → 3) (4,3-α-glucanotransferase) linkages can be formed. 19 Besides, the 4,6-α-GTase from Lactobacillus reuteri 121 has been used to produce isomalto/malto-polysaccharides (IMMPs) with a DP of up to 30. 22 These products contain one or more α(1 → 4)-linked glucosyl units at the reducing end, and at least one α(1 → 6) linkage at the non-reducing end.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic synthesis of polysaccharide-based copolymers

et al. 2018

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The design of enzymatic routes for the production of biosourced copolymers represents an attractive alternative to chemical synthesis from fossil carbon. In this paper, we explore the potential of glycosynthesizing enzymes to produce novel block copolymers composed of various covalently-linked α-glucans with contrasting structures and physicochemical properties. To this end, various glucansucrases able to synthesize α-glucans with different types of α-osidic bonds from sucrose were tested for their ability to elongate oligosaccharide and polysaccharide acceptors with different structures from the native polymer synthesized by each enzyme. We showed that two enzymes -namely, the alternansucrase from Leuconostoc mesenteroides NRRL B-1355 (specific for α(1 → 6)/α(1 → 3)-linked alternan synthesis) and the dextransucrase DSR-MΔ1 from Leuconostoc citreum NRRL B-1299 (specific for α(1 → 6)-linked dextran formation) -were able to elongate α(1 → 4)-linked amylose and α(1 → 6)/α(1 → 3)-linked alternan respectively. Carrying out stepwise acceptor reactions, and after optimization of the acceptor size and donor/acceptor ratio, two types of diblock copolymers were synthesized -a dextran-b-alternan and an alternan-b-amylose -as well as the triblock copolymer dextran-b-alternan-b-amylose. Their structural characterization, performed by combining chromatographic, NMR and permethylation analyses, showed that the copolymer polymerization degree ranged from 29 to 170, which is the highest degree of polymerization ever reported for an enzymatically synthesized polysaccharide-based copolymer. The addition of dextran and alternan blocks to amylose resulted in conformational modifications and related flexibility changes, as demonstrated by small angle X-ray scattering.

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4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H

Cited by 49 publications

References 61 publications

Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes

Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Enzymatic synthesis of polysaccharide-based copolymers

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