Study on the Inhibitory Mechanisms of Native Cellulose, Microcrystalline Cellulose, and Soluble Cellodextrin on α-Amylase and Amyloglucosidase.

The inhibitory effects of natural cellulose (NC), microcrystalline cellulose (MC), and soluble fiber dextrin (SC) on amylase activity have been established; however, the underlying mechanisms remain poorly understood. This study employed fluorescence spectroscopy and fluorescence thermodynamics to investigate the quenching parameters, thermodynamic properties, and quenching mechanisms of cellulose interactions with α-amylase and amyloglucosidase. Structural alterations in both enzymes were examined using synchronous fluorescence and UV-visible absorption spectroscopy. The results indicated that NC, MC, and SC primarily induced static quenching of fluorophores in α-amylase and amyloglucosidase. When addition of SC reached 3%, SC reduced the fluorescence intensity of tyrosine and tryptophan residues in α-amylase by 70.9% and 86.8%, and in amyloglucosidase by 43.7% and 46.5%, respectively. Increasing SC levels also decreased hydrophobicity around tyrosine and tryptophan in α-amylase. These findings provide insights into designing cellulose-based amylase inhibitors through structural modulation for developing low-glycemic index (GI) foods.