2011
DOI: 10.2478/s11756-011-0053-y
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In vitro synthesis of glycogen: the structure, properties, and physiological function of enzymatically-synthesized glycogen

Abstract: This review describes a new enzymatic method for in vitro glycogen synthesis and its structure and properties. In this method, short-chain amylose is used as the substrate for branching enzymes (BE, EC 2.4.1.18). Although a kidney bean BE and Bacillus cereus BE could not synthesize high-molecular weight glucan, BEs from 6 other bacterial sources produced enzymatically synthesized glycogen (ESG). The BE from Aquifex aeolicus was the most suitable for the production of glycogen with a weight-average molecular we… Show more

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Cited by 36 publications
(22 citation statements)
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“…Glycogen‐like hyperbranched α‐glucans have been reported to form in vitro upon action of a branching enzyme on short‐chain amylose as well as the tandem action of a branching enzyme and an amylosucrase enzyme on sucrose units, for example. These in vitro synthesized glycogens have different properties from native glycogen particles in terms of molecular weight, size distribution, and degradability.…”
Section: Functionalizing Glycogen Nanoparticlesmentioning
confidence: 99%
“…Glycogen‐like hyperbranched α‐glucans have been reported to form in vitro upon action of a branching enzyme on short‐chain amylose as well as the tandem action of a branching enzyme and an amylosucrase enzyme on sucrose units, for example. These in vitro synthesized glycogens have different properties from native glycogen particles in terms of molecular weight, size distribution, and degradability.…”
Section: Functionalizing Glycogen Nanoparticlesmentioning
confidence: 99%
“…For a high ratio (around 340), the synthesized chains are long and reorganize in the form of a random organization of crystallites by a retrogradation process (Fig. Two methods have been reported, described as "SP-GP-BE" (based on the use of sucrose phosphorylase (SP), '-glucan phosphorylase (GP), and branching enzyme (BE)) with sucrose and maltotetraose as substrates (Ohdan et al 2006;Kajiura et al 2011) and "IAM-BE-AM," in which the branched linkages of starch were first hydrolyzed by an isoamylase (IAM) to produce short amylose chains that were assembled into spherical particles by a branching enzyme (BE) and an amylomaltase (AM) (Kajiura et al 2008). For a low ratio (close to 1), small spikelike protrusions are seen on the surface (Fig.…”
Section: Enzymatic Modification Of Branched (14)˛(16)glucansmentioning
confidence: 99%
“…The enzyme that forms the basis of this strategy is 1,4-α-glucan branching enzyme (GBE, EC 2.4.1.18), which belongs to the α-amylase family. GBE is known to cleave the α-1,4 glucosidic linkage of an existing glucan chain and transfer the cut end to the 6-position of a glucose residue within the cleaved chain or within another glucan chain, creating an α-1,6 glucosidic linkage (Devillers, Piper, Ballicora, & Preiss, 2003;Kajiura et al, 2011). GBE has been widely used in previous studies to modify a variety of polysaccharides.…”
Section: Introductionmentioning
confidence: 99%