Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
Burgeoning scientific literature proves that enzymes can catalyze chemical reactions in non-conventional media, are active against liquid, solid or gaseous substrates, retain their catalytic function in organic solvents, biphasic systems composed of organic solvent and water and supercritical fluids. Non-aqueous media appeared to be a promising alternative as an environment for the reactions catalyzed by enzymes. The possibility of carrying out enzymatic processes in such unusual milieus enlarged the range of applications of biocatalysis, and solved many problems witnessed by pharmaceutical, food and chemical industries. The paper describes both advantages and disadvantages of non-conventional media, and presents the examples of practical uses of selected enzymes (lipases, proteases, oxidoreductases, glycosidases) in these systems. The details on medium composition and the form of the biocatalyst are included.
EN
Enzymology of non-aqueous media, also termed a non-conventional enzymology, is a discipline focused on chemical reactions catalysed by enzymes in the media other than water. However, such environments always contain certain amount of water, either dissolved in a solvent or enzyme-bound. The latter fraction of water is called an essential one, and it is crucial for the non-aqueous enzymology, since it stabilises the conformation of protein molecule and determines its enzymatic activity. The paper presents structure, function, and methods of assays of the enzyme-bound water together with other water forms that can also be found in reaction milieu. The methods of regulation of enzymatic activity in non-aqueous media by using compounds capable of associating with polar atoms of amino acid residues involved in catalysis, and thus positively influencing activity of enzymes, have also been discussed. The factors giving rise to a decrease in catalytic activity of enzymes under non-aqueous conditions, and methods of prevention against this phenomenon have also been analysed.
EN
The embodiment of subtilisin from Bacillus subtilis IBTC-3 in triacetylocellulose (TAC) fibre was studied. The fibre preparation of proteolytic activity 51.3 AmU/g was obtained with 16.6% of yield. The properties of subtilisin embedded in TAC fibre were investigated. The preparation showed optimal proteolytic activity at pH 9 and temperature 65-70C. It was stable in a wider range of pH and temperature than the native subtilisin. The KM value for haemoglobin was 2.6 ? 10-3 M. The TAC-fibre biocatalyst, in the fixed bed column, was successfully applied for hydrolysis of casein.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.