Inhibition mechanism of α-amylase and amyloglucosidase by spherical nanocrystalline cellulose with varying particle sizes.
Journal:
International journal of biological macromolecules
Published Date:
May 8, 2025
Abstract
In this study, spherical nanocrystalline cellulose (SNC) was isolated from native cellulose through phosphoric acid hydrolysis and ultrasonic treatment. The spherical nanocrystalline cellulose with three particle sizes of 50 nm, 60 nm and 70 nm was studied using in vitro digestion experiments, enzyme activity inhibition experiments, fluorescence spectroscopy, synchronous spectroscopy, and circular dichroism spectroscopy. The results demonstrated that SNC markedly reduced enzymatic starch hydrolysis within the model system, with suppression efficacy inversely proportional to particle dimensions. SNC-50 (50 nm) demonstrated the highest inhibitory potency against α-amylase (IC: 0.93 mg/mL) and amyloglucosidase (IC: 1.61 mg/mL). Kinetic analyses revealed distinct inhibition modes: SNC induced non-competitive binding interference with α-amylase, while amyloglucosidase activity was attenuated via a mixed-type inhibition mechanism. Steady-state fluorescence studies show that SNC forms static complexes with α-amylase or amyloglucosidase through a spontaneous endotherm, a process predominantly governed by hydrophobic interactions. In addition, synchronized spectra and circular dichroism spectra further indicate that SNC and amylase change the secondary structure of the protein through hydrophobic interactions. This study shows that SNC effectively inhibits starch digestion by interacting with amylase, making it a superior inhibitor of α-amylase and amyloglucosidase, which helps lower post-meal blood sugar levels.
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