Methods of determining proteolytic activity in commercial samples of immobilized proteinase preparations

Белов, А.А.; Ignatyuk, T. E.; Ryl'tsev, V. V.

doi:10.1007/bf00767674

Pharm Chem J

1993

DOI: 10.1007/bf00767674

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Methods of determining proteolytic activity in commercial samples of immobilized proteinase preparations

А.А. Белов¹,

T. E. Ignatyuk²,

V. V. Ryl'tsev³

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Cited by 3 publications

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“…The protein content in the substrate was found with the Lowry-Hartree method [8]. The proteolytic activity was established with the Kunitz method based on Hammarsten hydrolysis of a 1% solution of casein in 1/15 M phosphate buffer (PB), pH 8.0 [9], and BArNa-amidase activity was determined with the method in [10] in the modification in [11] in a solution of 0.05 M TRIS*HCl (pH = 8).…”

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Development and study of the properties of textile materials containing proteolytic enzymes

et al. 2008

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The data reported here for native and immobilized enzymes show that the stabilization (or destabilization) effect changes as a function of the temperature, so that the term "stabilization" only has meaning for the concrete temperature conditions and the concrete enzyme [compare lysoamidase (LA) and trypsin (TR)]. For this reason, there are always two temperature regions in the general case -where the native or the modified enzyme is more stable [21]. The analysis of the times for cleansing wounds of suppurative-necrotic masses and complete healing showed that the immobilized forms of the enzymes were much more effective than the corresponding native preparations. This is because native (unmodified) enzymes are rapidly inactivated and washed out in wound discharges, while the immobilized preparations are more stable and have a lasting action. In addition, the therapeutic effect of the materials containing an enzyme complex (collitin -CL -or crab hepatopancreas -CP) is higher in comparison to monoenzymatic preparations (Tr, for example) [22,23].Proteolytic enzymes (trypsin, chymotrypsin, collagenase, etc.) are widely used in medicine [1][2][3][4]. In application on a suppurative-necrotic wound, proteolytic enzymes (PE) split, bringing nonviable tissues which must usually be removed with a scalpel to the soluble state [4]. The possibility of intracavitary, intramuscular, and in many cases also local administration is low due to the irritating effect of proteinases, their immunogenic and allergenic properties, hemolytic action in intravenous administration, poor bioavailability, and other factors manifested together or separately, but relatively frequently. Clinical use is limited by the high cost, low availability, rapid elimination from the body, and impossibility of creating a high local concentration of the preparation without increasing its systemic concentration. These drawbacks can be eliminated to a significant degree by chemical modification of the proteins with high-molecular-weight compounds, which allows reducing the total dose of the preparation used, increasing its time in the body, and simultaneously attenuating undesirable side effects -i.e., a high local concentration of the preparation can be attained with chemical modification, while the total dose will be negligibly small in comparison to use of the native protein [5].Relatively cheap proteinase complexes are preferred for industrial use in comparison to monoenzymatic preparations for many reasons; first, lower loss of overall activity during production; second, the most expensive and laborious stages of purification are eliminated (gel filtration and ion-exchange chromatography, etc.); third, the complexes have a broader spectrum of action both with respect to the pH range and with respect to substrate specificity [6].The Textile Materials Research Institute is the basic developer and manufacturer of textile materials containing various enzymes. These materials are used as applications, cotton wool, lint or powder, and as dressings for treatment...

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Development and study of the properties of textile materials containing proteolytic enzymes

et al. 2008

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“…The surface of fibers is activated with a bifunctional cross-linking agents, specifically glutaraldehyde which is suitable both for cellulose and polyamide fibers. Callulose fibers can be activated with oxidants to form dialdehyde cellulose [33,35]; surface grafting polymerization with acrylic acid is also possible [36]. In any case, the fiber surface acquires active chemical groups (as a rule, aldehyde) which react with surface functional groups of protease molecules to form strong covalent bonds.…”

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“…The overwhelming majority of protease-containing fibrous materials are produced by means of covalent immobilization [17,[33][34][35][36]. The surface of fibers is activated with a bifunctional cross-linking agents, specifically glutaraldehyde which is suitable both for cellulose and polyamide fibers.…”

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Immobilized proteases for wound cleaning

Vernikovskii

Степанова

2012

Russ J Gen Chem

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Biodegradation of Palisada perforata (Rhodophyceae) and Sargassum sp. (Phaeophyceae) biomass by crude enzyme preparations from algicolous fungi

et al. 2014

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Methods of determining proteolytic activity in commercial samples of immobilized proteinase preparations

Cited by 3 publications

References 1 publication

Development and study of the properties of textile materials containing proteolytic enzymes

Development and study of the properties of textile materials containing proteolytic enzymes

Immobilized proteases for wound cleaning

Biodegradation of Palisada perforata (Rhodophyceae) and Sargassum sp. (Phaeophyceae) biomass by crude enzyme preparations from algicolous fungi

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