acid-phosphatase has been researched along with goethite* in 3 studies
3 other study(ies) available for acid-phosphatase and goethite
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Enzymatic hydrolysis of organic phosphates adsorbed on mineral surfaces.
Esters of phosphoric acid constitute a sizable fraction of the total phosphorus supply in the environment and thus play an important role in the global phosphorus cycle. Enzymatic hydrolysis of these esters to produce orthophosphate is often a required reaction preceding phosphorus uptake by plants and microorganisms. Generally, adsorption to environmental particles is assumed to limit this process. Here we show, however, that the rate of enzymatic hydrolysis of glucose-1-phosphate (G1P) adsorbed on goethite by acid phosphatase (AcPase) can be of the same order of magnitude as in aqueous solution. The surface process releases carbon to the solution whereas orthophosphate remains adsorbed on goethite. This hydrolysis reaction is strictly an interfacial process governed by the properties of the interface. A high surface concentration of substrate mediates the formation of a catalytically active layer of AcPase, and although adsorption likely reduces the catalytic efficiency of the enzyme, this reduction is almost balanced by the fact that enzyme and substrate are concentrated at the mineral surfaces. Our results suggest that mineral surfaces with appropriate surface properties can be very effective in concentrating substrates and enzymes thereby creating microchemical environments of high enzymatic activity. Hence, also strongly adsorbed molecules in soils and aquatic environments may be subjected to biodegradation by extracellular enzymes. Topics: Acid Phosphatase; Adsorption; Biocatalysis; Biodegradation, Environmental; Glucose; Glucosephosphates; Hydrolysis; Iron Compounds; Minerals; Organophosphates; Solanum tuberosum; Solutions; Spectrophotometry, Infrared; Surface Properties | 2012 |
Adsorption, desorption and activities of acid phosphatase on various colloidal particles from an Ultisol.
Adsorption, desorption and activity of acid phosphatase on various soil colloidal particles and pure clay minerals were studied. Higher adsorption amounts and low percentage of desorption of acid phosphatase were found on fine soil clays (<0.2 microm). Electrostatic force and ligand exchange are the major driving forces that are involved in the adsorption of enzymes on soil clays. More enzyme molecules were adsorbed on soil clays in the presence of organic components. However, enzymes on organic clays were more easily released. One-third of the enzyme on goethite was adsorbed via ligand exchange process. Some other interactions, such as van der Waals force, hydrophobic force and hydrogen bonding may be more important in the adsorption of enzyme on kaolinite and the enzyme in this system cannot be easily removed. Coarse clays (0.2-2 microm) and inorganic soil clays had higher affinities for enzyme molecules than fine clays and organic clays, respectively. The activity of enzyme bound on soil clays was inhibited and the thermal stability was increased in the presence of organic matter. Data obtained in this study are helpful for a better understanding of the interactions of enzymes with inorganic and organic constituents in soil and associated environments. Topics: Acid Phosphatase; Adsorption; Aluminum Silicates; Clay; Colloids; Hydrogen-Ion Concentration; Iron Compounds; Kaolin; Ligands; Minerals; Particle Size; Sensitivity and Specificity; Soil; Surface Properties; Temperature | 2005 |
Effects of several low-molecular weight organic acids and phosphate on the adsorption of acid phosphatase by soil colloids and minerals.
Adsorption of acid phosphatase on goethite, kaolinite and two colloids from the soils in central and south China in the presence of organic acids and phosphate was studied. With the increase of anion concentration, the ability in decreasing enzyme adsorption followed the sequence: phosphate>tartrate>oxalate>acetate. Acetate showed promotive effect on enzyme adsorption at lower anion concentrations whereas oxalate, tartrate and phosphate compete effectively with enzyme in a broad range of anion concentration. The adsorption isotherms of enzyme in most of the anionic systems studied conformed to the Langmuir equation. Phosphate reduced the affinity of enzyme on goethite more significantly than the other anions. However, tartrate decreased the affinity of enzyme on soil colloids and kaolinite to a greater extent than phosphate, oxalate and acetate. This observation suggested that the impact of anions on enzyme adsorption varies with anionic type and the surface characteristics of soil components. The influence of the addition order of ligand on enzyme adsorption was found greater in tartrate and phosphate systems. In general, simultaneous introduction of ligand and enzyme into the system had the lowest enzyme adsorption, showing more competition between ligand and enzyme molecules in this system. Data from this work indicated that the status and activity of enzyme in certain soil microenvironments especially the rhizosphere where various organic and inorganic ligands are active can be altered and may be completely different from the bulk soil. Topics: Acid Phosphatase; Acids, Acyclic; Adsorption; Colloids; Iron Compounds; Kaolin; Minerals; Phosphates; Soil | 2003 |