Insights into the catalytic properties of 4,3-α-glucanotransferase to guide the biofabrication of α-glucans with low digestibility.

Abstract

The effect of the starch chain structure on 4,3-α-glucanotransferase's (4,3-α-GTase) catalytic properties was investigated to modulate the digestibility of starch. Three starches with diverse amylose contents were used, and the enzymatic kinetic reaction of 4,3-α-GTase was fitted using the Michaelis-Menten equation. The results revealed that the linear substrate was more suitable for modification by 4,3-α-GTase. Linear starch chains were then selected with various degrees of polymerization (DP) as substrates of 4,3-α-GTase modification. Additionally, the structures and in vitro digestion of 4,3-α-GTase derived α-glucans were studied. The results showed that enzyme catalysis increased the amount of α-1,3 glycosidic linkages in products (highest 33.5%), the digestibility of 4,3-α-GTase derived α-glucans conformed to a first-order two-phase equation, and the equilibrium digestibility was controlled between 43.2-72.1%. It was observed that the structure of α-glucans could be managed to attain low digestibilities (43.2%) by selecting maltodextrin with DE 2 as the substrate. These findings offer valuable insights into the fabrication of α-glucans and their potential applications in various fields.