Fine structural properties of natural and synthetic glycogens

Glycogen, highly branched (1→4)(1→6)-linked α-d-glucan, can be extracted from natural sources such as animal tissues or shellfish (natural source glycogen, NSG). Glycogen can also be synthesized in vitro from glucose-1-phosphate using the cooperative action of α-glucan phosphorylase (GP, EC 2.4.1.1) and branching enzyme (BE, EC 2.4.1.18), or from short-chain amylose by the cooperative action of BE and amylomaltase (AM, EC 2.4.1.25). It has been shown that enzymatically synthesized glycogen (ESG) has structural and physicochemical properties similar to those of NSG. In this study, the fine structures of ESG and NSG were analyzed using isoamylase and α-amylase. Isoamylase completely hydrolyzed the α-1,6 linkages of ESG and NSG. The unit-chain distribution (distribution of degrees of polymerization (DP) of α-1,4 linked chains) of ESG was slightly narrower than that of NSG. α-Amylase treatment revealed that initial profiles of hydrolyses of ESG and NSG were almost the same: both glycogens were digested slowly, compared with starch. The final products from NSG by α-amylase hydrolysis were glucose, maltose, maltotriose, branched oligosaccharides with DP ⩾ 4, and highly branched macrodextrin molecules with molecular weights of up to 10,000. When ESG was digested with excess amounts of α-amylase, much larger macrodextrins (molecular weight > 106) were detected. In contrast, oligosaccharides with DP 4-7 could not be detected from ESG. These results suggest that the α-1,6 linkages in ESG molecules are more regularly distributed than those in NSG molecules.

It has been shown that enzymatically-synthesized glycogen (ESG) has similar structural and physicochemical properties to natural source glycogen (NSG). However, hydrolysis of glycogens with an excess amount of alpha-amylase suggested a slight difference in the distribution of α-1,6 linkages in ESG and NSG molecules.Figure optionsDownload as PowerPoint slide