[Peroxidase oxidation of phenols]. / Peroksidaznoe okislenie fenolov.

Partially purified preparations of horseradish peroxidase were able to catalyze the effective transformation of such phenol compounds as phenol, o-chlorophenol, 2,4,6-trichlorophenol, pentachlorophenol (giving rise to the formation of polymer products insoluble in water), resorcinol, and thymol (giving rise to the formation of low-molecular-weight products). The following conditions were found to be optimal for peroxidase oxidation and provide the maximum extent of elimination of phenol compounds: temperature, 15-25 and 25-30 degrees C for phenol and chlorophenol compounds, respectively; molar ratio H2O2/phenol, 1:1; and transformation time, 1-3 h. Although effective transformation was observed within a broad range of pH, the efficiency of the process slightly increased at a pH from 6.0 to 7.5. It was suggested to carry out multiple peroxidase oxidations of phenols using partially purified peroxidase enclosed in a dialysis membrane bag placed into a solution of a phenol compound containing hydrogen peroxide.

[Reduction of nitro-substituted compounds by native and immobilized Escherichia coli cells]. / Vosstanovlenie nitrozameshchennykh soedinenii nativnymi i immobilizovannymi kletkami Escherichia coli.

Reduction of nitro-substituted compounds, 1,4-benzodiazepine-2-ones, dibenzo[b,f]-1,4-diazepines, quinolones, and quinoxalinones, by Escherichia coli cells was studied. Physicochemical methods demonstrated the formation of corresponding amines. 4-(p-Nitrophenyl)-1H-6-R-quinolones-2 were nor reduced by Escherichia coli cells. Regiospecific reduction of 2,4-dinitro-5H-11-(p-R-phenyl)-dibenzo[b,f]-1,4-diazepines and 4-(2'-R-3',5'-dinitro)-benzoyl-3,4-dihydroquinoxalinones-2 was shown to result in the formation of 2-nitro-4-amino-5H-11-(p-R-phenyl)-dibenzo[b,f]-1,4-diazepines and 4-(2'-R-3'-nitro-5'-amino)-benzoyl-3,4-dihydroquinoxalinones-2, respectively. Methods for microbiological reduction of nitro compounds and immobilization of Escherichia coli cells into carrageenan and its modified forms were elaborated.

[Immobilization of the lytic enzyme complex lysoricephine]. / Immobilizatsiia liticheskogo fermentnogo kompleksa lizoritsefina.

Entrapping of the lysoenzyme complex of lysoricephine in solutions of hydrophilic polymers and its immobilization on dressing materials were performed. Immobilized preparations that retained 80-100% of the lytic activity and stable during storage were obtained. Properties of the immobilized preparations: dependence on pH and temperature, stability in acidic medium, and effect of gamma-radiation were studied. It was shown that coimmobilization with protease C induced a 1.5-1.7-fold increase in the lytic activity of the immobilized preparation compared to the native enzyme complex of lysoricephine.

[The immobilization of proteolytic enzymes on carbon materials]. / Immobilizatsiia proteoliticheskikh fermentov na ugol'nykh materialakh.

Immobilization of proteolytic enzymes on carbon materials depends on the concentration of the protein to be immobilized, the protein/carrier ratio and pH. The kinetics of the proteolytic enzyme adsorption and combined immobilization of proteases and lytic enzymes are considered, and properties of the resultant preparations (temperature and pH optima) and the effect of gamma-sterilization are discussed. Chymotrypsin and terrilytin immobilized on carbon SKN-2P hydrolysed 0.2% solution of casein during 25-27 days with a maximum yield of 50-70%.

[Reduction of nitro-substituted 1,2-dihydro-3H-1,4-benzodiazepine- 2-ones by E. coli cells immobilized in carrageenan]. / Vosstanovlenie nitrozameshchennykh 1,2-digidro-3H-1,4-benzdiazepin-2- onov kletkami E. coli, immobilizovannymi v karraginan.

Reduction of nitro-substituted 1,2-dihydro-3H-1,3-benzodiazepine-2-ones by E. coli cells immobilized in carrageenan was studied. The corresponding amines are the sole products with a 100% yield as compared to the native cells. Conditions for immobilization of E. coli cells in the home-produced carrageenan was worked out: the cell to carrageenan ratio is 1:10 (w/w), granulation in toluene at 0-(+)4 degrees, treatment with 0.3-0.4 M KCl. The carrageenan-immobilized cells are stable upon storage, repeated usage (after 10 cycles about 80% of the initial activity is retained), and when being used in column fermenters.

[Treatment of experimental suppurative wounds with proteolytic and lytic enzymes immobilized on carbonic cloth]. / Lechenie gnoinykh ran proteoliticheskimi i liticheskimi fermentami, immobilizovannymi na ugol'noi tkani, v éksperimente.

When in the experiment on rats the jointly immobilized on a carbonic cloth proteases and lytic enzyme complex were used, the reduced period of the suppurative wound cleaning and healing was noted as compared to that in use of the immobilized on a carbonic cloth proteases and jointly immobilized on a gause proteases and lytic enzyme complex.

[The selective reduction of nitro compounds by E. coli cells]. / Izbiratel'noe vosstanovlenie nitrosoedinenii kletkami E. coli.

Nitroreduction of 2,4-dinitro-5H-11-p-R-phenyl-[b,f]-1,4-diazepines and 4-(2'-R-3',5'-dinitro)benzoyl-3,4-dihydroquinoxalinones-2 by E. coli with formation of 2-nitro-4-amino-11-p-R-phenyldibenzo-[b,f]-1,4-diazepines and 4-(2'-R-3'-nitro-5'-amino)-benzoyl-3,4-dihydroquinoxalinones-2 has been demonstrated using a set of physical and chemical methods.

[Enzyme immobilization via silochromes, modified by transition metal salts]. / Immobilizatsiia fermentov na silokhromakh, modifitsirovannykh soliami perekhodnykh metallov.

The immobilization of pectoawamorine G 10X, pronase E and P, protease from Bac. mesentericus and rat liver microsomal fraction was performed by sylochromes modified by Ti, Zr and Hf salts. The pectinesterase, caseinolytic, esterase and hydroxylating activity of the immobilized preparations, their stability during storage, thermostability and pH optimum are determined. Of greatest interest for practical application are preparations of pectoawamorine. G 10X and pronase E and P immobilized by HfOCl2.

[Immobilization of pectawamorine G10x on silichromes]. / Immobilizatsiia pektavamorina G10x na silokhromakh.

Immobilization of pectawamorine G10x on silochromes, using cyanuric chloride, 2,4-toluylene diisocyanate, glutaric dialdehyde, thionyl chloride, phosphorus tribromide, titanium tetrachloride, zirconium oxychloride and hafnium oxychloride was studied. The use of glutaric dialdehyde assured the strongest binding and the preatest stability of activity. Properties of the native pectawamorine G10x and immobilized preparations were studied on a comparative basis. Pectawamorine G10x immobilized by means of hafnium oxychloride showed increased stability when stored at 5 degrees C and used repeatedly. In every case, except for cyanuric chloride and glutaric dialdehyde, maximum activity was at a temperature 10 degrees C higher than for the native enzyme, and optimum pH varied for the preparations with different binding reagents.

[Immobilization of pectawamorine G10x by gel entrapment]. / Immobilizatsiia pektavamorina G10x vkliucheniem v gel'.

Polyacrylamide gel immobilization of pectawamorine G10x was investigated. Its pectinesterase and polygalacturonase activity and stability in storage were measured. The degree of pectawamorine binding during gel immobilization was 80--90%, 55% of initial activity being retained. Thermal stability of the immobilized and native preparations was equal. Pectinesterase activity of the gel immobilized enzyme increased during storage.

[Pronase E and P immobilization on aminoorganosilica surface]. / Immobilizatsiia pronazy e i p na poverkhnosti aminoorganokremiezema.

Immobilization of pronase E and P was performed on sylochrome modified by gamma-aminopropyltrietoxysilane using cyanuric chloride, 2,4--toluylenediisocyanate, glutaric aldehyde and also on sylochrome by means of titanium tetrachloride. The esterase and caséinolytic activities of the immobilized preparations and their stability during storage were determined. The increased thermostability of the immobilized preparation is established. The influence of the enzyme: carrier ratio on the immobilization process and activity of the enzymes was studied. It is shown that application of glutaric aldehyde favours the best retention of the esterase activity (73%), whereas the caseinolytic activity is better retained (31%) when titanium tetrachloride was used.

[Application of immobilized animal liver microsomal fraction to the reaction of 1,4-benzdiazepine-2-one conversion]. / Ispol'zovanie immobilizovannoi fraktsii mikrosom pecheni zhivotiykh dlia reaktsii prevrascheniia 1,4-benzdiazepin-2-onov.

The albino rat strain Wistar and Shynashylla rabbit liver microsomal fraction was immobilized by incorporation into polyacrylamide gel. It is shown, that the microsomal fraction immobilized by such a method catalyzes the hydrolysis of 1,4-benzdiazepine-2 ones, 3-acetoxyderivatives, hydroxylation in position 3 of 1,4-benzdiazepine-2-ones and reduction of nitrazepame. The storage thermostability and stability of the immobilized preparations were studied. Immobilization of the animal liver microsomal fraction was conducted on sylochrome by cyanuric chloride and 2,4-toluylenediisocyanate.