Title
Multi-spectral and thermodynamic analysis of the interaction mechanism between Cu2+ and α-amylase and impact on sludge hydrolysis
Author
Ruiqi Zhou, Hong Liu, Guangying Hou, Lei Ju, Chunguang Liu
Year
2017
Journal
Environmental Science and Pollution Research
Abstract
An increasing amount of heavy metals (e.g., Cu2+) is being discharged into sewage treatment plants and is accumulating in sludge, which is toxic to the enzyme in sludge or soil when the sludge is used as fertilizer, resulting in unfavorable effect on the biological treatment of sludge and the circulation and conversion of materials in soil. In this research, effect of Cu2+ on sludge hydrolysis by α-amylase is studied from the respect of concentration and components of soluble organic matter in sludge, using three-dimensional fluorescence spectra. Results show that Cu2+exposure not only inhibits the hydrolysis of sludge due to the denaturation of α-amylase but also affects the components of soluble organic matter in sludge. In order to illuminate the interaction mechanism between Cu2+ and α-amylase (a model of hydrolase in sludge), multi-spectra and isothermal titration microcalorimetry techniques are applied. Results show that the secondary structure of α-amylase is changed as that the α-helical content increases and the structure loosens. The microenvironment of amino acid residue in α-amylase is changed that the hydrophobicity decreases and the polarity increases with Cu2+ exposure. Isothermal titration calorimetry results show that Van der Waals force and hydrogen bond exist in the interaction between Cu2+ and α-amylase. Results from this research would favor the development of advanced process for the biological treatment of sludge containing heavy metals.
Instrument
J-810
Keywords
Circular dichroism, Secondary structure, Ligand binding, Biochemistry