Abstract
Humic acids (HA) are one of the main environmental factors controlling the fate and behavior of the compounds released into the environment. In particular, they are universally considered of great importance in determining soil extracellular enzyme activity and stability via association with essential soil enzymes. The objective of this study was to investigate the interaction of coal HA with an extracellular multicopper oxidase laccase (EC 1.10.3.2) that catalyze the oxidation of a wide range of reducing substances in the environment. Using size-exclusion chromatography analysis and monitoring laccase activity, the formation of a stable and an enzymatically active complex between HA and laccase was shown. Basing the data obtained by isoelectric focusing of HA-laccase complex, non-covalent character of laccase association with HA was considered and binding of laccase to HA by weak dispersive forces such as van der Waals, hydrophobic, π-π, CH-π and others was hypothesized.
Highlights
Humic substances (HS) are ubiquitous natural compounds comprising the major component of soil organic matter and sediments, as well as aquifers [1,2,3]
They are universally considered of great importance in determining soil extracellular enzyme activity and stability via association with essential soil enzymes such as ureases, proteases, phosphatases, hydrolases, laccases, and peroxidases, which have been detected in soil extracts as complexes with HS [4,5]
Size-Exclusion Chromatography (SEC)-profiles of Humic acids (HA) and laccase solely did not change within 72 hours (Figure 1) demonstrating their stability during the time of the experiment
Summary
Humic substances (HS) are ubiquitous natural compounds comprising the major component of soil organic matter and sediments, as well as aquifers [1,2,3]. HS are one of the main environmental factors controlling the fate and behavior of the compounds released into the environment They are universally considered of great importance in determining soil extracellular enzyme activity and stability via association with essential soil enzymes such as ureases, proteases, phosphatases, hydrolases, laccases, and peroxidases, which have been detected in soil extracts as complexes with HS [4,5]. Laccases (EC 1.10.3.2) are extracellular multicopper oxidases that catalyze the oxidation of a wide range of reducing substances with the concomitant reduction of O2 Because of their capability of oxidizing aromatic compounds, such as phenols and anilines, laccases have promising potential as industrial enzymes for various applications, such as wood fiber modification, biosensor construction, and water and soil remediation [6,7,8,9,10]. The objective of this research was to investigate laccase interaction with HS in a model system containing laccase and coal humic acids (HA) and to get insight into the nature of HA-laccase complex
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