New enzymatic immobilized biocatalysts for detoxification of organophosphorus compounds

Ефременко, Елена; Peregudov, Аlexander S.; Кильдеева, Н. Р.; Perminov, P. A.; Varfolomeyev, S.D.

doi:10.1080/10242420500132474

Cited by 20 publications

(11 citation statements)

References 21 publications

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“…Thus, substrate specificity of polypeptides was not affected by chosen type of immobilization. The comparison of catalytic efficiency of the biocatalysts obtained via our method to the known analogs produced by other methods [7,[11][12] revealed the obvious advantages of our chosen immobilization technique and its components ( Table 1). The comparison of catalytic activities of known immobilized biocatalysts, based on OPH with genetically introduced affinity tags (440 U for OPH/GFP-OPH [14] and 0.0025 U for ELP-OPH [15]) to the same parameters of newly developed preparation (660 U) revealed the latter one's advantage.…”

Section: Resultsmentioning

confidence: 95%

“…A stable form of OPH for repeated application in OPC hydrolysis is usually obtained via immobilization of the enzyme [7][8][9][10], and there have been a number of various approaches to enzyme immobilization in the development of effective biocatalysts with OPH activity suitable for flow systems [11][12][13]. The use of various amino acid sequences genetically introduced into OPH structure as ligands for enzyme immobilization proved to be an advanced and very effective method for biocatalyst production [14][15].…”

Section: Introductionmentioning

confidence: 99%

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Dried–Reswollen Immobilized Biocatalysts for Detoxification of Organophosphorous Compounds in the Flow Systems

Ефременко

Lyagin

Plieva

et al. 2009

Appl Biochem Biotechnol

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New immobilized biocatalysts based on polypeptides containing N- or C-terminal polyhistidine sequences and possessing organophosphorus hydrolase activity were investigated for detoxification of organophosphorous neurotoxic compounds in the flow systems. The biocatalysts were revealed to have a high catalytic activity within wide pH and temperature ranges 7.5-12.5 degrees C and 15-65 degrees C, respectively. The immobilized biocatalysts can be dried and reswollen before use with 92-93% catalytic activity remaining after drying and rehydration procedures. The half-lives of the biocatalysts under wet and dry storage conditions were 420 and 540 days, respectively.

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Section: Resultsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Dried–Reswollen Immobilized Biocatalysts for Detoxification of Organophosphorous Compounds in the Flow Systems

Ефременко

Lyagin

Plieva

et al. 2009

Appl Biochem Biotechnol

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“…As a rule, enzyme immobilization makes it more stable. 21,22 This communication describes an attempt to change characteristics of the enzyme containing an N termi nal hexahistidine tag (His 6 OPH) 23,24 by introducing 3 fluorotyrosine into the protein molecule.…”

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confidence: 99%

Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase

2006

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“…Kinetics of the change in the modulus of elasticity of chitosan gels crosslinked with GA at pH 4.1 (1-3), 5.6 (4, 5), GA/NH 2 ratio of 0.415 (4), 1.049(2,3,5), and 2.517 mole/mole (1) and concentration of chitosan of 1.31 (1, 2, 4, 5) and 1.62%(3).…”

mentioning

confidence: 99%

“…Compositions based on chitosan solutions containing trypsin and the calculated amount of GA were used for forming a gel membrane on the surface of coarse calico [5].…”

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confidence: 99%

Crosslinking in solutions of chitosan in the presence of a crosslinking reagent for production of fibre biocatalysts

2006

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541.64:547.458 and N. R. Kildeeva Gelation in soltuion sof chitosan in the prfesence of a bifunctional crosslinking reagent of glutaraldehyde and protein was investigated. It was shown that the gelation rate, strength, and equilibrium moisture absorption fo the gel formed are determined by the conditions of crosslinking the chitosan (MW of chitosan, pH, and GA/NH 2 ratio). The systems studied were used in fabrication of fibre biocvatalysts by pformation of an enzyme-containing gel membrane on the surface of coarse calico.Of the natural polysaccharides, chitosan is in second place after cellulose with respect to distribution and industrial use. The increased interest in this aminopolysaccharide is due to its properties: biocompatibility, susceptibility to enzymatic hydrolysis, intrinsic physiological activity combined with nontoxicity, ability to bind some organic compounds, heavy metal ions, etc. For these reasons, chitosan is used in medicine, agriculture, the food industry, and manufacture of cosmetics [1].The features of the chemical structure of chitosan are responsible for its solubility in acid aqueous media, which significantly reduces the environmental stress in manufacture and facilitates its processing into different polymer forms: films, fibres, membranes, and capsules. At the same time, the solubility of the finished articles made from chitosan, films in particular, is frequently a drawback, so that these articles are heated or treated with modifying reagents: diisocyanates, sulfuric acid, glutaraldehyde (GA), etc., to increase resistance to dissolution. Glutaraldehyde is a very common crosslinking reagent long used for immobilizing proteins [2]. In addition to reducing the solubility of chitosan, intermolecular crosslinking at amino groups [3, 4] allows covalently adding proteins to chitosan, enzymes in particular, to obtain heterogeneous biocatalysts.Chitosan manufactured by Bioprogress Closed Joint-Stock Company (Shchelkovo) with a molecular weight (MW) of 170 and 840 kDa and degree of deacetylation of 0.92 in the form of 2% solutions in 2% acetic acid was used to study the features of crosslinking of chitosan by GA; the pH of freshly prepared solutions of chitosan was 4.1. To establish the effect of the pH on the features of gelation, potentiometric titration of a solution of chitosan with MW of 170 kDa was conducted with a concentrated solution of NaOH to pH 5.6, which is 0.1 less than the cloud point. The reaction of chitosan and GA was studied at a 1.31% concentration of chitosan in the reaction mixture, and the GA/NH 2 ratio was adjusted by varying the concentration of the GA solution (Merck). The kinetics of the change in the viscosity of the solution was investigated on a Rheotest 2 flow viscometer using a coneplane measuring device which allowed giving the shear rate and fixing the stresses that develop in the system with low consumption of reagents. The kinetics of the change in the modulus of elasticity of crosslinked chitosan gels was investigated with penetration of a spherical ind...

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New enzymatic immobilized biocatalysts for detoxification of organophosphorus compounds

Cited by 20 publications

References 21 publications

Dried–Reswollen Immobilized Biocatalysts for Detoxification of Organophosphorous Compounds in the Flow Systems

Dried–Reswollen Immobilized Biocatalysts for Detoxification of Organophosphorous Compounds in the Flow Systems

Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase

Crosslinking in solutions of chitosan in the presence of a crosslinking reagent for production of fibre biocatalysts

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