Molecular mechanisms of interaction between enzymes and Maillard reaction products formed from thermal hydrolysis pretreatment of waste activated sludge. (1st November 2021)

• Record Type: Journal Article
• Authors: Wang, Qiandi; Xu, Qiongying; Wang, Huidi; Han, Bo; Xia, Dasha; Wang, Dongsheng; Zhang, Weijun
• Is Part Of: Water research. Volume 206(2021)
• Publication Date: 2021-11-01
• Subjects: Waste activated sludge -- Thermal hydrolysis pretreatment -- Anaerobic digestion -- Maillard reaction products -- Enzyme activity -- Molecular interaction; Water -- Pollution -- Research -- Periodicals; 363.7394
• DOI: 10.1016/j.watres.2021.117777
• Languages: English
• ISSNs: 0043-1354

Abstract

Highlights: The presence of MRPs significantly inhibited the activity of extracellular lysozyme. The MRPs-lysozyme interaction is a spontaneous exothermic process. Aromatic structures with polar N atoms in MRPs interacted strongly with proteins. H-bond and aromatic stacking occurred simultaneously in MRPs-Lysozyme complex. The changes in protein secondary structure mainly contributed to enzyme activity decrease. Abstract: Thermal hydrolysis pretreatment (THP) is often used to improve the anaerobic digestion performance of waste activated sludge (WAS) in wastewater treatment plants (WWTPs). During the THP process, the proteins and polysaccharides in the biomass will undergo hydrolysis and Maillard reaction, producing biorefractory organic substances, such as recalcitrant dissolved organic nitrogen (rDON) and melanoidins. In this study, a series of spectroscopy methods were used to quantitatively analyze the Maillard reaction of glucose and lysine, and the interaction mechanisms of the Maillard reaction products (MRPs) and lysozyme were investigated. Results showed that the typical aromatic heterocyclic structures in MRPs, such as pyrazine and furan, were found to quench molecular fluorescence of lysozyme, resulting in an unfolding of standard protein structure and increase in lysozyme hydrophobicity. Significant loss of enzyme activity was detected during this process. Thermodynamic parameters obtained from isothermal titration calorimetry (ITC) confirmed that the interaction between MRPs and lysozyme occurred both exothermically and spontaneously. Density functional theory (DFT) calculations suggested that the molecular interactions of MRPs and protein included parallel dislocation aromatic stacking, T-shaped vertical aromatic stacking, H-bond and H-bond coupled to aromatic stacking. Graphical abstract: Image, graphical abstract