An Investigation of Enzymatic Phosphorolysis of α(1→4)-Linked Oligo-d-glucosaminides by Thermostable α-Glucan Phosphorylase Catalysis

α-Glucan phosphorylases (α-GPs) catalyze the reversible phosphorolysis of α-1,4-linked polysaccharides such as glycogen, starch, and maltodextrins, therefore playing a central role in the usage of storage polysaccharides. The discovery of these enzymes and their role in the course of catalytic conversion of glycogen was rewarded with the Nobel Prize in Physiology or Medicine in 1947. Nowadays, however, thermostable representatives attract special attention due to their vast potential in the enzymatic production of diverse carbohydrates and derivatives such as (functional) oligo- and (non-natural) polysaccharides, artificial starch, glycosides, and nucleotide sugars. One of the most recently explored utilizations of α-GPs is their role in the multi-enzymatic process of energy production stored in carbohydrate biobatteries. Regardless of their use, thermostable α-GPs offer significant advantages and facilitated bioprocess design due to their high operational temperatures. Here, we present an overview and comparison of up-to-date characterized thermostable α-GPs with a special focus on their reported biotechnological applications.

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Thermostable alpha-glucan phosphorylases: characteristics and industrial applications

Ubiparip

Beerens

Franceus

et al. 2018

Appl Microbiol Biotechnol

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Synthesis and functionalization of glucan dendrimer, and its application as a drug delivery system carrier

Yanase

Kuriki

2021

Amylase

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Glycogen is a natural polysaccharide with a dendrimer structure, in which glucose is frequently branched and polymerized. Functionalizing the numerous non-reducing ends on the molecular surface of glycogen could be expected to enable its use in various fields. We developed a method for enzymatically synthesizing a suitable form of glycogen from sucrose by using sucrose phosphorylase and branching enzyme, both of which belong to the α-amylase family, as well as glucan phosphorylase. We refer to this enzymatically synthesized glycogen as the glucan dendrimer (GD). We then selectively modified the non-reducing ends on the surface of GD particles by using the reaction of glucan phosphorylase with various hexose 1-phosphates. Modifying the non-reducing ends of GD with glucuronic acid or glucosamine added negative and positive charges to the GD particles. In addition, we found that glucuronic acid and/or glucosamine residues at the non-reducing ends can be used to covalently conjugate functional substances, such as sugar chains, proteins, and peptides to the surface of GD particles. GD and modification of its non-reducing ends represent versatile platforms for pharmaceutical applications of polysaccharides.

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An Investigation of Enzymatic Phosphorolysis of α(1→4)-Linked Oligo-d-glucosaminides by Thermostable α-Glucan Phosphorylase Catalysis

Abstract: n +Glc-1-P. Under the conditions in the large donor/acceptor ratios, successive glucosylations at the elongating nonreducing end from maltooligosaccharide as a primer take place by α-glucan

Cited by 2 publications

References 25 publications

Thermostable alpha-glucan phosphorylases: characteristics and industrial applications

Thermostable alpha-glucan phosphorylases: characteristics and industrial applications

Synthesis and functionalization of glucan dendrimer, and its application as a drug delivery system carrier

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