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An exploration of the interaction mechanism of Direct Red 80 with α‐Amylase at the molecular level
Author(s) -
Song Yan,
Sun Kailun,
Liu Rutao
Publication year - 2021
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2883
Subject(s) - amylase , chemistry , enzyme , hydrogen bond , docking (animal) , enzyme assay , exothermic process , biophysics , nuclear chemistry , adsorption , molecule , biochemistry , organic chemistry , biology , medicine , nursing
The use and production of Direct Red 80 (DR80) dye are growing rapidly, and a large amount of dye wastewater is discharged into the soil without treatment. DR80 accumulated in soil or sludge can lead to enzyme poisoning, inhibit microbial activity, and affect the transformation of substances in the soil. In this research, the interaction mechanism between DR80 and α‐Amylase (a typical enzyme in soil and sludge) was investigated by multi‐spectra, molecular docking, thermodynamics analysis and enzyme activity experiment. The results of UV‐visible and resonance light scattering (RLS) spectra showed that the skeleton of α‐Amylase became loosened and unfolded under the exposure of Direct Red. The size of α‐Amylase was smaller and α‐Amylase became dispersed under high concentration of DR80. Molecular docking and thermodynamic analysis showed that DR80 bound to the surface of domain A rather than the active site of α‐Amylase in the form of hydrogen bonds, and the binding process was an exothermic reaction. In addition, the inhibition of α‐Amylase activity by DR80 was verified by enzyme activity experiment. These results indicate that DR80 has an effect on the structure and function of α‐Amylase at molecular level, which means that the toxicity of DR80 should receive more attention.