Applying the Sabatier Principle to Decipher the Surface-Structure-Dependent Catalysis of Different Starch Granules by Pullulanase.

ABSTRACT: Interfacial enzyme catalysis is widespread in both nature and industry. Granular starch is a sustainable and abundant raw material for which a rigorous correlation of the surface structure with enzymatic degradation is lacking. Here pullulanase-catalyzed debranching of 12 granular starches varying in amylopectin contents and branch chain contents and lengths is shown to present a biphasic relationship characteristic of the Sabatier principle. Introducing normalization of the specific rate (v ₀/E ₀) by a substrate-dependent constant C, related to the Arrhenius prefactor of k _cat, reveals that optimal activity according to the Sabatier principle occurs at moderate substrate binding strength. The density of pullulanase attack sites

SUBMITTER: Wang Y 

PROVIDER: S-EPMC11775686 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature