Biomedical subjects
Publications and source records attributed to J Zemek.
The ability to degrade oligo- and polysaccharides by enzymes of the glycosidase and glucan-glucan hydrolyse type, and esterase, phosphatase, proteinase, peroxidase, catalase, laccase and tyrosinase activities were tested in 35 strains of 11 sections of the genus Fusarium.
Comparative investigations were carried out concerning substrate specificity and action patterns of seven Bacillus-endo-beta-glucanases produced by the species, B. subtilis, B. macerans, B. amyloliquefaciens, B. circulans, B. laterosporus, B. pumilus and B. polymyxa. All enzymes with the exception of beta-glucanase from B. macerans hydrolyze lichenan and barley-beta-glucan only and were without action on laminaran and CM-cellulose. It was suggested that hydrolysis products of beta-glucanase produced by B. macerans were markedly different from the products of the other enzymes. We conclude that B. macerans enzyme, which cleaves laminaran and beta-1,3-1,4-glucans, represents "laminarinase" type (1-3-beta-D-glucan glucanohydrolase, E.C. 3.2.1.6). On the other hand the glucanases produced by the other Bacillus strains belong to "licheninases" 1-3,1-4-beta-D-glucan glucanohydrolases, E.C. 3.2.1.73).
Production of beta-1,3-1,4-glucan hydrolase (licheninase) was studied in 45 strains of Bacillus representing 17 various species using lichenin as substrate. It was found that the enzyme was produced by the strains of B. pumilus, B. subtilis, B. amyloliquefaciens, B. polymyxa, B. macerans, B. laterosporus and one strain of B. circulans. A new screening method based on application of a gel prepared from the cross-linked lichenin as an only source of carbon in the cultivation medium is presented. Using this method and methods using other cross-linked gels as carbon sources in a synthetic liquid medium, production of licheninase, amylase and cellulase by the strains tested is compared.
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The antibacterial effect of 19 4-nitrophenylhydrazones, isonicotinoylhydrazones, and N-4-nitrophenylhydrazones, of 9 mono- and 2 disaccharides was tested with Micrococcus luteus, Bacillus licheniformis and Escherichia coli.
Inhibitory effects of compounds with guaiacyl and syringyl structure, representing the structure of native lignin, were studied on model cultures of bacteria, yeasts, yeast-like microorganisms and moulds. Isoeugenol exhibited the most pronounced inhibitory effect on growth of the studied microorganisms.
The biosynthesis of starch was investigated in the reaction catalyzed by plant alpha(1 leads to 4)-glucan phosphorylase using alpha-D-glucopyranosyl phosphate and its deoxy analogues as substrates. It was found that the hydroxyl groups at the positions C-2, C-3, C-4 and C-6 in the glucose moiety of the molecule of alpha-D-glucopyranosyl phosphate are not essential for its substrate properties in the transglycosylic reaction. The affinity of plant (alpha(1 leads to 4)-glucan phosphorylase and the rate of hexose incorporation into alpha(1 leads to 4)-glucan decreases in the following sequence: alpha-D-glucopyranosyl phos-phosphate, 2-deoxy-, 6-deoxy, 4-deoxy, and 3-deoxy-alpha-D-glucopyranosyl phosphate. The deoxyglucosyl analogues of alpha-D-glucosylpyranosyl phosphate act as competitive inhibitors on the elongation reaction of the alpha(1 leads to 4) chains of starch. It was found that more than one residue of 2-deoxy-D-glucose or 6-deoxy-D-glucose can be incorporated into the nonreducing terminus of alpha(1 leads to 4)-glucan chains of starch.
Of a total of 177 strains of yeasts and yeast-like organisms only 8 were capable of producing alpha-amylase; most strains were able to utilize 1,4-alpha-glucans by means of enzymes acting on the non-reducing ends of the outer glucan chains.
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The biosynthesis of alpha,alpha'-trehalose was investigated in a reaction catalyzed with yeast UDP-Glc :glucose-6-phosphate 1-glucosyl transferase. It was revealed that the hydroxyls at positions C-2, C-3, C-4 and C-6 are not essential for preserving its substrate properties in this reaction. The affinity of the enzyme and the rate of hexose incorporation into trehalose decreases in following sequence: UDP-glucose, UDP-2-deoxy-D-glucose, UDP-6-deoxy-d-glucose, UDP-4-deoxy-D-glucose and UDP-3-deoxy-D-glucose.
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The inhibitory effect of molybdenum ions on growth of yeasts at pH 5.5 was found to be decreased by aldoses in the following order: D-talose greater than L-mannose greater than L-ribose greater than D-lyxose greater than L-galactose greater than L-arabinose greater than L-glucose greater than L-xylose. Increased concentrations of molybdenum brought about morphological changes of yeast cells. Cells grown under these conditions were smaller, had thicker walls and formed clusters.
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