Thermostable α-Glucan Phosphorylase-catalyzed Successive α-Mannosylations

Shimohigoshi, Riko; Takemoto, Yasutaka; Yamamoto, Katsuhiro; Kadokawa, Jun‐ichi

doi:10.1246/cl.130286

Cited by 19 publications

(9 citation statements)

References 29 publications

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“…Previous studies involved a glycosyltransferase, 10,40 a glycosidephosphorylase, [12][13][14][15] or transglycosidases, 22,41 and produced either statistical copolymers or co-oligomers (of a total size of less than 30 glycosyl units) rather than block copolymers. Here, we demonstrated that the selected glucansucrases (DSR-M and ASR) transfer α-glucosyl residues to acceptor polymers (i) with a conformation and linkage composition different from that of their natural acceptors, and (ii) a size of up to 30 glucosyl residues, producing copolymers comprising up to 171 residues.…”

Section: Discussionmentioning

confidence: 99%

“…[12][13][14][15] The substrate promiscuity of this enzyme towards glycosyl donors (α-D-Glc-1-phosphate, α-DGlcNAc-1-phosphate and α-D-Man-1-phosphate) was exploited to produce non-natural polysaccharides such as hetero-mannosides and aminopolysaccharides. [13][14][15] The three sugar-phosphate donors were used in the presence of a maltotriose acceptor to obtain different copolymers with maltotriose at the reducing end, on which were grafted α(1 → 4)-mannan, α(1 → 4)-linked glucosaminoglucans or heteromannans (composed of either Glc and GlcNAc units, or Glc and Man units). Nevertheless, the degree of polymerization of the products was limited to 30 residues, 14 with a very short block of only three glucosyl residues at the reducing end.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enzymatic synthesis of polysaccharide-based copolymers

et al. 2018

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“…Glucoamylase hydrolytic studies showed that xylose was added to the nonreducing end of the obtained heterooligosaccharide. The authors further extended this method to the preparation of N-formylα-glucosaminylated maltooligosaccharide, 60 α-glucuronylated maltooligosaccharide, 61 α-mannosylated maltooligosaccharide, 62 chitin and chitosan stereoisomers, 63 and non-natural heteroaminopolysaccharides. 64 A further example of enzymatic synthesis of a hetero-oligosaccharide was reported by the same research group.…”

Section: Kadokawa Et Al First Established This Methodsmentioning

confidence: 99%

Amylose engineering: phosphorylase‐catalyzed polymerization of functional saccharide primers for glycobiomaterials

Nishimura

Akiyoshi

2016

WIREs Nanomed Nanobiotechnol

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Interest in amylose and its hybrids has grown over many decades, and a great deal of work has been devoted to developing methods for designing functional amylose hybrids. In this context, phosphorylase‐catalyzed polymerization shows considerable promise as a tool for preparing diverse amylose hybrids. Recently, advances have been made in the chemoenzymatic synthesis and characterization of amylose‐block‐polymers, amylose‐graft‐polymers, amylose‐modified surfaces, hetero‐oligosaccharides, and cellodextrin hybrids. Many of these saccharides provide clear opportunities for advances in biomaterials because of their biocompatibility and biodegradability. Important developments in bioapplications of amylose hybrids have also been made, and such newly developed amylose hybrids will help promote the development of new generations of glyco materials. WIREs Nanomed Nanobiotechnol 2017, 9:e1423. doi: 10.1002/wnan.1423For further resources related to this article, please visit the WIREs website.

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“…Taking the different recognition behavior of thermostable GP (from Aquifex aeolicus VF5) from potato into account, it has been found that the former enzyme catalyzed a different reaction manner from the latter enzyme when Man-1-P or GlcN-1-P was used as a glycosyl donor. When the thermostable GP-catalyzed glycosylation of Glc 3 acceptor with Man-1-P or GlcN-1-P was carried out in acetate buffer, consecutive glycosylations took place to obtain non-natural heterooligosaccharides composed of α(1→4)-linked Man/GlcN chains [55]. The MALDI-TOF mass spectra of the products with 10:1 donor/acceptor feed ratio showed several peaks corresponding to the molecular masses of tetra~hepta-octa-saccharides having one-four or five Man or GlcN residues with Glc 3 ( Figure 5).…”

Section: Thermostable Gp-catalyzed Enzymatic Oligomerization and Polymentioning

confidence: 99%

α-Glucan Phosphorylase-Catalyzed Enzymatic Reactions Using Analog Substrates to Synthesize Non-Natural Oligo- and Polysaccharides

Kadokawa

2018

Catalysts

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As natural oligo- and polysaccharides are important biomass resources and exhibit vital biological functions, non-natural oligo- and polysaccharides with a well-defined structure can be expected to act as new functional materials with specific natures and properties. α-Glucan phosphorylase (GP) is one of the enzymes that have been used as catalysts for practical synthesis of oligo- and polysaccharides. By means of weak specificity for the recognition of substrates by GP, non-natural oligo- and polysaccharides has precisely been synthesized. GP-catalyzed enzymatic glycosylations using several analog substrates as glycosyl donors have been carried out to produce oligosaccharides having different monosaccharide residues at the non-reducing end. Glycogen, a highly branched natural polysaccharide, has been used as the polymeric glycosyl acceptor and primer for the GP-catalyzed glycosylation and polymerization to obtain glycogen-based non-natural polysaccharide materials. Under the conditions of removal of inorganic phosphate, thermostable GP-catalyzed enzymatic polymerization of analog monomers occurred to give amylose analog polysaccharides.

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Thermostable α-Glucan Phosphorylase-catalyzed Successive α-Mannosylations

Cited by 19 publications

References 29 publications

Enzymatic synthesis of polysaccharide-based copolymers

Enzymatic synthesis of polysaccharide-based copolymers

Amylose engineering: phosphorylase‐catalyzed polymerization of functional saccharide primers for glycobiomaterials

α-Glucan Phosphorylase-Catalyzed Enzymatic Reactions Using Analog Substrates to Synthesize Non-Natural Oligo- and Polysaccharides

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