Binding affinity and adhesion force of organophosphate hydrolase enzyme with soil particles related to the isoelectric point of the enzyme

Islam, Shah Md. Asraful; Yeasmin, Shabina; Islam, Md. Saiful; Islam, Md. Shariful

doi:10.1016/j.ecoenv.2017.03.010

Cited by 10 publications

(4 citation statements)

References 31 publications

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“…Soil clays–enzyme complexes play an important role in the fate of organic chemicals entering the environment. Organic chemicals enter the soil environment either by deliberate actions such as pesticide or herbicide application, waste disposal and contaminants in soil amendments or accidentally by chemical spills, storage facility leakage (Islam et al, ; Northcot & Jones, ). Furthermore, research have shown that many chemicals form persistent and essentially permanently bound residues in soil (Northcot & Jones, ).…”

Section: Discussionmentioning

confidence: 99%

“…The AFM three‐dimensional images of the samples were taken, under similar conditions, with a XE‐Series AFM (Park Systems corp. Suwon, Korea) in air and at room temperature (23°C). The scanner was of type 910 M‐NSC36 and had a size of 4 μm in thickness and 30 μm in width as shown in our previous study by Islam, Yeasmin, Islam, and Islam (). A silicon nitride cantilever with a spring constant of 0.01–3 Nm was used in contact mode and the scanning frequency was 22.0 Hz.…”

Section: Methodsmentioning

confidence: 99%

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Modeling the clay minerals–enzyme binding by fusion fluorescent proteins and under atomic force microscope

Math

Reddy

Yun

et al. 2019

Microscopy Res & Technique

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In the present study, binding of cellulase protein to different clay minerals were tested using fluorescent–protein complex and microscopic techniques. Cellulase gene (Cel5H) was cloned into three fluorescent vectors and expressed as fusion enzymes. Binding of Cel5H–mineral particles was confirmed by confocal microscopy, and enzyme assay. Among the Cel5H–fusion enzymes, green–fusion enzyme showed higher intensity compared with other red and yellow fusion–proteins. Intensity of fusion–proteins was dependent on the pH of the medium. Confocal microscopy revealed binding of the all three fusion proteins with different clay minerals. However, montmorillonite displayed higher binding capacity than kaolinite clay. Likewise, atomic force microscopy (AFM) image profile analysis showed proteins appeared globular molecules in free‐state on mica surface with an average cross sectional diameter of 110 ± 2 nm and rough surface of montmorillonite made protein appear flattened due to structural alteration. Even surface of kaolinite also exerted some strain on protein molecular conformation after binding to surface. Our results provide further evidence for 3D visualization of enzyme–soil complex and encourage furthering study of the force involved interactions. Therefore, our results indicate that binding of proteins to clay minerals was external and provides a molecular method to observe the interaction of clay minerals–enzyme complex.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Modeling the clay minerals–enzyme binding by fusion fluorescent proteins and under atomic force microscope

Math

Reddy

Yun

et al. 2019

Microscopy Res & Technique

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“…Pesticide is widely used to kill pests, but only a small fraction (<1%) of the pesticide is actually applied to destroy pests. Due to its high toxicity and inappropriate disposal, pesticide residues in the environment have caused a serious threat to human health. − According to the WHO, an average of 3 million people suffer from pesticide poisoning each year, and more than 200 thousand people die from pesticides . Therefore, it is necessary to degrade those pesticides residues.…”

Section: Introductionmentioning

confidence: 99%

Simple Purification and Immobilization of His-Tagged Organophosphohydrolase from Cell Culture Supernatant by Metal Organic Frameworks for Degradation of Organophosphorus Pesticides

Xue

Zhou

et al. 2019

J. Agric. Food Chem.

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Coordinating unsaturated metal sites (CUS) on the surface of metal–organic frameworks (MOFs) could be used to adsorb His-tagged proteins. The specific adsorption between CUS and His-tagged proteins could reduce preparation steps, shorten preparation time, and could also avoid the binding between the metal ion of metalloenzyme active center and the chelating agent to ensure the enzyme activity. In this study, MIL-88A was synthesized by hydrothermal method and used to purify and immobilize His-tagged organophosphohydrolase (OpdA) in one step for organophosphate bioremediation. Under optimized conditions, OpdA@MIL-88A had a maximal activity of 1554 U/gprotein, which was nearly 5 times higher than free OpdA. Compared with free OpdA, OpdA@MIL-88A exhibited improved organic solvent tolerance, SDS tolerance, thermal stability, and storage stability. OpdA@MIL-88A was used to degrade organophosphorus pesticides on grapes and cucumbers. After reuse 6 times, OpdA@MIL-88A retained more than 66% and 61% of the initial activity, respectively. Therefore, this proposed strategy provided a facile and effective method for degradation of organophosphorus pesticides.

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“…AFM, a powerful tool used for single-molecule interaction between protein-ligand (Sumbul and Rico 2019 ), clay minerals-protein (Math et al 2019 ), affinity under in-vitro conditions and protein-substrates like cellulose (Liu et al 2020 ). Also, rupture forces of cellulose binding module and fiber substrates of cellulose, were measured using AFM (Griffo et al 2019 ), and an adhesive force were successfully measured between pesticide degrading enzyme-soil particles (Islam et al 2017 ). These exclusive evidences motivated us to use AFM to understand molecular mechanism and measure the adhesive forces involved between clay minerals-protein in current study.…”

Section: Introductionmentioning

confidence: 99%

Role of Cel5H protein surface amino acids in binding with clay minerals and measurements of its forces

et al. 2021

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Our previous study on the binding activity between Cel5H and clay minerals showed highest binding efficiency among other cellulase enzymes cloned. Here, based on previous studies, we hypothesized that the positive amino acids on the surface of Cel5H protein may play an important role in binding to clay surfaces. To examine this, protein sequences of Bacillus licheniformis Cel5H (BlCel5H) and Paenibacillus polymyxa Cel5A (PpCel5A) were analyzed and then selected amino acids were mutated. These mutated proteins were investigated for binding activity and force measurement via atomic force microscopy (AFM). A total of seven amino acids which are only present in BlCel5H but not in PpCel5A were selected for mutational studies and the positive residues which are present in both were omitted. Of the seven selected surface lysine residues, only three mutants K196A(M2), K54A(M3) and K157T(M4) showed 12%, 7% and 8% less clay mineral binding ability, respectively compared with wild-type. The probable reason why other mutants did not show altered binding efficiency might be due to relative location of amino acids on the protein surface. Meanwhile, measurement of adhesion forces on mica sheets showed a well-defined maximum at 69 ± 19 pN for wild-type, 58 ± 19 pN for M2, 53 ± 19 pN for M3, and 49 ± 19 pN for M4 proteins. Hence, our results demonstrated that relative location of surface amino acids of Cel5H protein especially positive charged amino acids are important in the process of clay mineral-protein binding interaction through electrostatic exchange of charges.

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Binding affinity and adhesion force of organophosphate hydrolase enzyme with soil particles related to the isoelectric point of the enzyme

Cited by 10 publications

References 31 publications

Modeling the clay minerals–enzyme binding by fusion fluorescent proteins and under atomic force microscope

Modeling the clay minerals–enzyme binding by fusion fluorescent proteins and under atomic force microscope

Simple Purification and Immobilization of His-Tagged Organophosphohydrolase from Cell Culture Supernatant by Metal Organic Frameworks for Degradation of Organophosphorus Pesticides

Role of Cel5H protein surface amino acids in binding with clay minerals and measurements of its forces

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