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1

Enzymatic synthesis of oligosaccharides

100%
S. B. S., Buchowiecka A., Gajewska M.
Biotechnologia
|
1999
|
issue 1
67-83
EN
A key role of oligosaccharides in biological processes becoming more obvious every day. An increasing interest in this group of biomolecules is related to their broad spectrum of applications, i.e. in food, feed and pharmaceutical industries, in cosmetics and medicine. Efficient, full-scale processes that allow to produce different types of these oligomers are of graet importance. Biocatalysis is considered very attractive in comparison to the non specific, time-consuming and often environmental unfriendly chemical technologies of oligosaccharide production. Two groups of enzymes are involved in this process, transferases and glycosidase. This review describes oligosaccharide synthesis through the reactions of transfer, transglycosylation and reverse hydrolysis.
2

Characterization of bacteria of the genus Thermus and their biotechnological importance

88%
Sinkiewicz I., Synowiecki J.
Biotechnologia
|
2009
|
issue 3
148-162
EN
Gram-negative, aerobic bacteria of the genus Thermus which have been isolated from many natural and artificial, thermal environments are used as a source of thermostable restriction nucleases and DNA polymerase, as well as can be exploited for the production of many other enzymes with a great industrial importance. The strains belonging to the genus Thermus utilize carbohydrates, amino acids, carboxylic acids and peptides and their optimal growth temperatures ranged from 55 to 85oC. This review is focused on the adaptation of Thermus strains to thermostability and on characterisation and possible application of their enzymes.
3

Selected issues of non-conventional enzymology. Part II ? Characterization of reaction media and biocatalysts applied in non-conventional enzymology

88%
Antczak T., Szczesna-Antczak M.
Biotechnologia
|
2003
|
issue 3
139-158
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.
4

The activity of chitin deacetylase and glycosidases of the crude enzyme extracts of Mucor rouxii mycelium

75%
Kolodziejska I., Wojtasz-Pajak A., Malesa-Ciecwierz M., Niecikowska C.
Biotechnologia
|
1997
|
issue 2
158-169
EN
The crude enzyme extract obtained from Mucor rouxii had optimal deacetylasde activity against chitosan acetylated in 39% in the Ph range of 5,2-5.9. Its activity against watger-soluble chitoologosaccharides, containing from 3 to 6 N-acetylglucosamine residues, was the higest in respect to (GlcNAc)s and nil against substrates containing less than 4 N-acetylglucosamine residues.Crystaline chitin was resistant to the deacetylase and to glycosidases present in the extract; amorphous chitin was noticeably more susceptible to these enzymes.Chitosan in the form of suspension was slightly deacetylated and hydrolysed by enzyme extracts.Solubilized chitosan acetylated in 39% was mostly susceptible to enzymatic deacetylation.The deacetylase activity in the extracts was inversely related and the chitonolytic activity was proportional to the deacetylation degree of soluble chitosan.
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