Advances in the study of the interface between enzymes/proteins and soil components.

Minerals, organic matter and so on are important solid-phase components of soil, which constitute the soil active interface, modulating the migration and transformation of heavy metals, organic pollutants, biomoleculars and so on in the soil.
soil enzymes/proteins are more adsorbed to soil organic matter, minerals, organic matter-mineral complexes.
this paper summarizes the adsorption mechanism of enzyme/protein on the interface and its main influencing factors, analyzes the bioactivity of adsorption-protein,protein, the change of conformation, and the intrinsic correlation between conformational change and biological activity, summarizes the main research methods of enzyme/protein and interface, and looks forward to the process and mechanism of molecular simulation technology on the enzyme/protein and soil interface, and fixation enzyme as an environmental material for the degradation of organic pollutants. Most of the
soil enzymes are proteins, mainly from the secretions of microorganisms and plant roots, as well as animal and plant residues, as an important component of the ecosystem, which is the biocatalyst of the ecosystem and the metabolic power of soil organisms.
these enzymes participate in the biochemical circulation of soil with carbon, nitrogen, phosphorus, sulfur and other elements, and are the implementers of soil organic matter conversion and the active reservoir of plant nutrients, whose activity is closely related to soil physical and chemical properties, soil types, fertilization, farming and other agricultural measures.
soil enzymes can reflect the direction and intensity of various biochemical processes, often as an important indicator of soil fertility and self-purification ability, because of its sensitivity to changes in environmental factors, but also as an early warning indicator of changes in soil ecosystem.
human activities will also directly or indirectly release various proteins into the soil, such as genetically modified crops can be root secretions and straw back to the soil to release Bt protein, some pathogenic proteins (prion virus, avian influenza virus, etc.) can also enter the soil environment through animals, threatening human health.
the soil solution has less free-state enzyme/protein content, and is present in the soil in the form of compounds in the soil component interface, including minerals, organic matter, mineral-organic compounds and so on.
minerals, organic matter, mineral-organic compounds, etc. form an important chemical interface in the soil, directly affecting the distribution, morphology, migration and transformation of nitrogen, phosphorus and other nutrients, organic matter, biomoleculars, etc.
enzyme/protein adsorption on the soil interface may be accompanied by changes in its conformation, and for bioactive enzymes/protein molecules, their activity and stability may also change during the chemical reactions involved in the interface.
the change of enzyme/protein molecular conformation may be one of the important factors affecting its activity and stability, but the mechanism of the change of conformation on biological activity is still unclear and needs further study.
1 Enzyme/Protein's Role in soil Interface 1.1 Prion virus, Bt toxin interface action in soil is the pathogen of infectious spongiform encephalopathy, which can enter the soil by infecting animal urine, feces, saliva or rotting carcasses, and the role of the soil component can affect the spread of the pathogenic protein, bio-fertility and persistence in the soil.
the interface between prion virus and model oxide (Al2O3, SiO2) is dominated by static power, the role of both depends largely on pH and ion strength, and the prion virus in the soil is more likely to interact with positively charged ferro-aluminum oxides.
, as a natural polyanion, is widely present in soil and water, not only has a strong affinity with prion virus, but also can increase the absorption capacity of mineral to prion virus.
the prion virus after the action of rotting acid is still infectious, but it can slow the rate of infection of the disease.
to assess the level of transmission in the soil and the accessibility of organisms after burial of infected animal carcasses, Jacobson and others used protease to treat infected brain tissue homogenization, using synthetic rain water as a rins, to simulate its ability to migrate in 5 different soils, resulting in the removal of the prion virus in the shampoo, the pathogenic protein is basically retained in the original location, may become an infectious source of infection with other organisms.
there is still a lack of effective inactivated soil prion virus methods, Chesney and other recent studies have found that the sulphate on methionine and tryptophan residues have oxidation, as a new way to repair the prion virus contaminated soil in situ.
Bt toxin can be released into the soil by genetically modified crops through root secretions, straw return to the field, etc., and interact with the various components of the soil.
Sander et al. and Madliger et al. studied the effects of pH and ion strength on the adsorption of Bt toxins on SiO2 and polylylylythine (PLL), and the results showed that electrostatic force was the driving force of the dominant Bt toxin adsorption, with the initial adsorption rate and adsorption on SiO2 with p The increase and decrease of the H value is the opposite of the adsorption result on the PLL, when the Bt toxin is charged the same as the adsorption interface, the adsorption increases with the decrease in ion strength, and the Bt toxin attached to SiO2 still has high insecticidal activity and maintains high structural stability during the adsorption desorption process.
soil, the rotting phytic acid as a natural organic matter, combined with Bt toxin seismometers through static power, hydrophobic action, the role between the two is affected by solution conditions (pH, ion strength), rotting acid polarity and surface charge, even when pH?gt;6 (greater than bt toxins such as electro-point) and When the ion strength decreases, the electrostatic action between the area of the positive charge of the Bt toxin and the negative charge rotting phytic acid still promotes the increase of the adsorption of the Bt toxin, the surface polarity of the rotting phytic acid is uneven, and the hydrophobic force makes the Bt toxin have a strong affinity for the area with higher corrosion phytic acid non-polarity.
1.2 enzymes/proteins play an important role in the application of enzymes/proteins in the soil interface, static power and hydrophobic action.
enzymes/proteins are biopolymer electrolyte molecules with gender charge, and the electrostatic action produced by the affinity interface is an important driving force for its adsorption to the hydrophilic interface, which varies with the change of ambient pH.
a positively charged lysozyme can enter and extend between the opposite charged montrock layers under the traction of electrostatic gravity, and the spatial barrier effect of Al(OH)x reduces the amount of lysozyme sesame incoming layers with the increase of al(OH) x covered by the surface of monditus.
driven by electrostatic gravity, the lysozyme is rotting phytic acid wrap in a three-dimensional mesh structure, which hinders the binding of substrate molecules and active sites.
when the enzyme/protein has the same charge as the solid surface, the hydrophobic action between the two also promotes the adsorption of the enzyme/protein, which becomes another important driving force for its adsorption.
water-repellent groups of layersiliated minerals and organic matter can be combined with hydrophobic hydrophobic areas with hydrophobic ally."
pH is 6, insulin, ribnuclease and the surface of the rotting acid are all negatively charged, hydrophobic can promote the encapsulation of the enzyme by overcoming electrostatic rejection between molecules.
the adsorption of The Bt toxin decreases with the increase of the perishant polarity of the rotting acid, and the adsorption amount of immunoglobulin, etc. increases with the enhancement of the hydrophobic properties of the interface, which proves the importance of hydrophobic action in the protein adsorption process. the roles between
enzymes/proteins and soil components also include position exchange, hydrogen bonds, Vanderwai, cation exchange, etc.
Huang and others studied the adsorption, desorption and enzyme activity of acidic phosphatase in different particles and minerals, and the results showed that nearly one-third of the acidphos phosphatase attached to the needle ore mainly combined with the ligand exchange, and the action between the kaolin sorgimmers to Van der Wael, hydrogen bonds, hydrophopha mainly, and therefore not easy to desphlic.
the adsorption of peroxidase and lyucinase in
is positively correlated with the amount of cation exchange, indicating that cation exchange may be one of the important mechanisms of interaction between the two.
1.3 The research method of soil enzyme/protein interface reaction is currently, the method of studying the interaction between enzymes/proteins and interfaces mainly includes several in Table 1. In addition to the differential reduction method, the adsorption of
enzyme/protein is also used for the determination of adsorption by isotope tracer, spheroidal polarity, microcrystalline balance and light waveguide pattern spectrum. The advantage of the
isotope tracing method is that it can be used for multi-component analysis, and the spheroidal spectrometry method can be used to determine the mass and thickness of the surface adsorption material by determining the state change of the surface material to the polarized light reflection, and the adsorption protein can be predicted according to the concentration of surface adsorption protein and the thickness of the adsorption layer. The state has been used for in situ detection of various surface enzyme/protein adsorption and resuction processes, and microcrystalline and light waveguide pattern stuble can not only determine protein adsorption, but also provide protein adsorption and desorption process information, which has been widely used in recent years in the study of enzyme/protein interaction with rotting acid.
, the change of adsorption-state enzyme/protein structure can be determined by Furie infrared spectroscopy, fluorescence spectrum, nuclear magnetic resonance, round bichromat spectrum and other methods (see 4.2), and the change of heat in enzyme/protein adsorption and desorption can be measured by micro-heat method and differential scanning thermal determination. the physical and chemical properties of the physical and chemical interface of the
2 enzyme/protein adsorption on the soil interface mainly include surface structure, hydrophobic properties, charge-electricity, etc.
the physical structure of the interface can have an effect on the adsorption of enzymes/proteins, Lundqvist and other studies of the adsorption of dehydrated enzymes on surfaces with different curvature SiO2, the results show that the enzyme has a strong interaction with particles with a larger diameter, resulting in a large change in the secondary structure of the enzyme molecule.
affected by the hydrophobic properties of the interface, fibrinogen and so on in the hydrophobic surface of hydrophobic faster adsorption rate than hydroxyl surface hydrophilic water.
McClellan and other studies have found that the thickness and density of the adsorption layer formed by bovine serum albumin in hydrophobic interfaces is about half the amount of adsorption in the hydrophilic interface, indicating that the role between protein molecules and hydrophobic interfaces is stronger and protein molecules are more denatured.
the adsorption results of proteinonatorine on different hydrophobic interfaces show that the amount of protein adsorption increases with the increase of interface hydrophobic properties (i.e., -CH3, -OPh3,- -CONHCH3), and the role between protein and interface is also enhanced.
2.2 enzyme/protein physical and chemical properties of enzymes/proteins in the interface adsorption is also related to its molecular weight, shape, surface energy group, charge, structural stability and so on.
, the stability of enzyme/protein structure is also an important factor affecting enzyme/protein adsorption.
polysocososomes, rnanuclease and other hard protein internal stability is high, in the hydrophilic surface adsorption is small, and the hydrophilic surface encounter seismonotating gravity can make the protein molecular structure change, resulting in increased adsorption;
2.3 solution conditions such as pH, ion strength, enzyme/protein concentration, can affect the amount of enzyme/protein adsorption, as well as the degree of variation in the arrangement and structure on the adsorption interface. Figure 1
is a diagram of the adsorption of a gender protein on the silica/water interface with the pH value and protein concentration.
pH has a greater effect on enzyme/protein adsorption, Mori and other studies have shown that when the solution pH is 3 (lower than the bSA or other electric point), the positively charged bovine serum albumin quickly adsorption to the clostular surface, but the electrostatic rejection between molecules causes the protein to be a single molecule adsorption layer on the solid surface, and when the pH is 6 (higher than the cell surface) the kinetic force between the protein and the cloud cell surface causes the kinelectric absorption of the protein.
protein concentration is another important reason to affect its distribution on the interface, when the protein concentration is low, its adsorption speed on the interface is slower, can be fully spread on the interface, and the force between the interface is enhanced.
when the concentration of bovine serum albumin is less than 0.5 g. L-1 and pH 3-7, the protein forms a uniform single layer adsorption on the interface, when its concentration is higher than 0.5 g. L-1 and the solution pH value reaches near the protein isoelectric point (pH 5.1), bovine serum albumin on the hydrophilic silica adsorption volume is the largest. the influence of
ion strength on enzyme/protein adsorption mainly depends on the charged properties of enzymes/proteins and interfaces, when the protein and the adsorption interface are charged with the same amount, there is static repulsion between the two, when the ion strength of the solution is increased, the electrostatic rejection force decreases, causing the enzyme/protein adsorption on the interface to increase;
3 interface effect on enzyme/protein biological characteristics 3.1 interface action on enzyme/protein activity after the enzyme/protein into the soil, combined with organic matter, minerals, mineral-organic complex, soil colloid, the degree of activity and stability change sesame with enzyme/protein type, interface type, environmental conditions and other factors. The activity of
adsorption-state enzyme is different because of its different types, lacquer enzyme and peroxidase adsorption on kaolin, monitase can maintain higher activity, and the phosphatase activity after adsorption is reduced, glucose oxidase adsorption to Kaolin, xylalkyamine-Montestone, its activity is no significant change.
different adsorption interfaces have different effects on soil enzyme/protein activity (Table 2), such as Bt protein adsorption to Kaolin stone after the insecticidal activity is significantly higher than montedestone, and insecticidal activity is also related to the proportion of soil media and protein.
the order in which the minerals inhibit the activity of acidic phosphatase and reparase are Montediator and Kaolin stone, the activity of the lustox adsorption on Them, aluminum hydroxide, montedite-aluminum hydroxide compound is Montedite and montitude-aluminum hydroxide, and the anti-hydroxie surface is reduced due to the aluminum-covereding, luxerase. the activity of
-corrosion phytic acid is promoted by the activity of conversion enzyme and acid phosphatase, and the effect on the activity of the enzyme and acid phosphatase is related to the molecular weight of the rotting acid itself, the pH of the solution and so on.
Marzadori et al. studied two different molecular weights of huminic acid HA1 (100-3).