α-L-rhamnosidase from Penicillium tardum and Its Application for Biotransformation of Citrus Rhamnosides.

Enzymatic deramnosylation of flavonoids is a convenient tool for improving the quality of citrus juices. α-L-rhamnosidase with a specific activity of 33.1 units/mg was isolated and characterized from the culture liquid of Penicillium tardum.

Lipopolysaccharide of Pantoea agglomerans 7460: O-specific polysaccharide and lipid A structures and biological activity.

Lipopolysaccharide (LPS) was isolated from Pantoea agglomerans 7460 cells by phenol-water extraction. Mild acid degradation allowed to separate OPS and lipid A. Lipid A was analyzed by negative-ion mode ESI MS and found to consist mainly of hexaacylated derivative containing biphosphorylated GlcN disaccharide, four 14:0 (3-OH), 18:0 and 12:0 fatty acids.

Structure of O-Polysaccharide and Lipid A of 8488.

The 8488 lipopolysaccharide (LPS) was isolated, purified and characterized by monosaccharide and fatty acid analysis. The O-polysaccharide and lipid A components of the LPS were separated by mild acid degradation. Lipid A was studied by electrospray ionization mass spectrometry (ESI-MS) and found to consist of hexa-, penta-, tetra- and tri-acylated species.

Development and characterization of chitosan/polyvinyl alcohol polymer material with elastolytic and collagenolytic activities.

The biologically active polymeric material with entrapped peptidase Bacillus thuringiensis var. israelensis with caseinolytic, collagenase and elastase activities was developed as a promising product for medical use. We have evaluated and reported here the following physical-chemical and biochemical characteristics of entrapped enzyme: peptidase/polymer interaction and morphology analyses, film thickness, water content, time of dissolution in water and physiological saline, kinetic of casein hydrolysis and pH- and thermoprofiles of proteolytic activity.

Pantoea agglomerans P1a lipopolysaccharide: Structure of the O-specific polysaccharide and lipid A and biological activity.

O-specific polysaccharide and lipid A were obtained from the lipopolysaccharide from new strain of Рantoea agglomerans P1a by mild acid hydrolysis. It was found that the major form of lipid A presented by tetraacylated derivative containing biphosphorylated GlcN disaccharide, three 14:0 (3-OH) and 12:0 residues. The structure of the O-specific polysaccharide was established by chemical, NMR and computational methods: →3)-α-D-Manp-(1 → 4)-β-D-Fucp-(1 → 4)-ɑ-D-Fucp-(1→The LPS of Р.

Lipopolysaccharides of Pantoea agglomerans 7604 and 8674 with structurally related O-polysaccharide chains: Chemical identification and biological properties.

Structurally related O-specific polysaccharide (O-antigen) and lipid A components were obtained by mild acid degradation of the lipopolysaccharides (LPSs) of two strains of bacteria Pantoea agglomerans, 7604 and 8674. Studies by sugar analysis along with 1D and 2D H and C NMR spectroscopy enabled elucidation of the following structures of the O-polysaccharides, which differ only in the linkage configuration of a side-chain glucose residue: R=α-d-Glcp in strain 7604 or β-d-Glcp in strain 8674 Lipid A samples were studied by GC-MS and high-resolution ESI-MS and found to be represented by penta- and tetra-acyl species; lipid A of strain 8674 also included hexaacyl species. A peculiar feature of lipid A of both strains is the presence of the major cis-9-hexadecenoic (palmitoleic) acid, which has not been found in P.

Purification and Characterization of a Naringinase from Cryptococcus albidus.

Naringinase which was extracted from the fermented broth of Cryptococcus albidus was purified about 42-folds with yield 0.7% by sulfate fractionation and chromatography on Toyopearl HW-60, Fractogel DEAE-650-s, and Sepharose 6B columns. Molecular weight of protein determined by gel filtration and SDS-PAGE was 50 kDa.

Lipopolysaccharide of Pantoea agglomerans 7969: Chemical identification, function and biological activity.

Lipopolysaccharide (LPS) of Pantoea agglomerans 7969 isolated from apple tree was purified and characterized chemically by sugar and fatty acid analysis. Lipid A was analysed by negative-ion mode ESI MS and found to consist mainly of hexa- and tetra-acyl species typical of E. coli lipid A.

Structure, Function and Biological Activity of Lipopolysaccharide Lipid A.

Bacterial lipopolysaccharides (LPS) are the major outer surface membrane components present in almost all gram-negative bacteria. It consists of poly- or oligosaccharide region that is anchored in the outer membrane by a specific lipid moiety termed lipid A. Recent studies have shown that it is only the lipid A of LPS that has the function of endotoxin.

[Screening of Mannane-Degrading Enzymes Producers].

The aim of research was to investigate the prevalence of complex mannan-degrading enzymes among museum and freshly isolated cultures of micromycetes, actinobacteria and bacteria. It has been shown that the producers of β-mannanases mostly extracted from sources that are rich in plant residues. We detected strains of Penicillium aculeatum, P.

Structure of the O-specific polysaccharides of Pseudomonas chlororaphis subsp. chlororaphis UCM B-106.

O-specific polysaccharide was obtained from the lipopolysaccharide of Pseudomonas chlororaphis subsp. chlororaphis UCM B-106 and studied by composition analysis along with 1D and 2D (1)H and (13)C NMR spectroscopy. The polysaccharide was found to contain a derivative of pseudaminic acid (Pse) and the following structure of the trisaccharide repeating unit was established: →4)-β-Psep5Ac7Hb-(2 → 6)-β-d-Galf-(1 → 3)-β-d-Galp-(1→ where Pse5Ac7Hb indicates 5-acetamido-3,5,7,9-tetradeoxy-7-[(R)-3-hydroxybutanoylamino]-l-glycero-l-manno-non-2-ulosonic acid.

[Screening of α-L-Rhamnosidases and Peptidases among Actinobacterium and Bacilli].

Purpose: To carry out screening of peptidases and α-L-rhamnosidases producers among actinobacterium and bacilli.

Methods: The biochemical methods of α-L-rhamnosidase, elastase, caseinolytic, fibrinolytic and collagenase activity determination have been used.

Results: Among 31 strains of actinobacterium and 24 strains of bacilli it was not exhibited any enzyme with elactolytic activity, while a number of actinobacterium strains displayed high collagenase activity.

[Functional and Biological Activity of Pantoea agglomerans Lipopolysaccharides].

The lipopolysaccharides (LPS) of the seven strains of Pantoea agglomerans were isolated and chemically identified. It was established that the investigated strains characterized by different relative output of LPS from 5.2 to 14.

Isolation and purification of Bacillus thuringiensis var. israelensis IМV В-7465 peptidase with specificity toward elastin and collagen.

Peptidase of Bacillus thuringiensis var. israelensis IМV В-7465 was isolated from culture supernatant using consecutive fractionations by an ammonium sulphate (60% saturation), ion-exchange chromatography and gel-filtration on the TSK-gels Toyoperl HW-55 and DEAE 650(M). Specific elastase (442 U∙mg of protein-1) and collagenase (212.

[Characterization of the Lipopolysaccharides of Pseudomonas chlororaphis].

Lipopolysaccharides (LPS) from two strains ot Pseudomonas chlororaphis subsp. aureofaciens,UCM B-111 and UCM B-306, were isolated and characterized. The LPS preparations exhibited low toxicity, high pyrogenicity and high antiviral activity.

[Screening of the Producents of α-L-Rhamnosidases Amongst Representatives of Penicillium].

The aim of this work was to study α-L-rhamnosidase [КФ 3.2.1.

[The Effect of Metal Ions and Chemical Reagents on the Activity of Achromobacter sp. 7a α-Amylase].

The effect of cations and anions on the activity of Achromobacter sp. 7a α-amylase was studied. It is shown that tested enzyme is stable to most of anions, however sensitive to a number of cations.

[SEROLOGICAL PROPERTIES AND BIOLOGICAL ACTIVITY OF PANTOEA AGGLOMERANS LIPOPOLYSACCHARIDES].

The serological and phytotoxic properties of lipopolysaccharide (LPS) of plant pathogens--Pantoea agglomerans were studied. It is known that the thin variations in the structure of the O-specific polysaccharides determining serological specificity of gram- negative bacteria and used as a molecular basis of serological classification schemes. For P.

[Physico-Chemical Properties of Achromobacter SP. α-Amylase].

From Achromobacter sp. 7a, that was isolated with Black sea, aquatoria of island Zmi- inyi, was isolated enzyme with α-amylase activity, that able also to split the synthetic substrates: p-nitrophenyl-α-D-glucopyranoside and p-nitrophenyl-α, -β-D-xylopyranoside. Methods of isolation and purification of enzyme were selected which included: ammonium sulfate precipitation and affinity sorption on starch, that improved enzyme activity in 7 times in comparison with activity in the supernatant of cultural liquid.

[PURIFICATION AND PHYSICO-CHEMICAL PROPERTIES OF PENICILLIUM TARDUM a-L- RHAMNOSIDASE].

By ammonium sulfate fractionation and chromatography on TSK-gels Toyopearl HW- 60 and Fractogel TSK DEAE-650-s from supernantant of cultural liquid of Penicillium tardum 1MB F-100074 was isolated and purified in 23 times preparation of enzyme with α-L-rhamnosidase activity with yield of 3.12 %. The specific activity was 27.

STABILITY OF NATIVE AND MODIFIED α-GALACTOSIDASE OF Cladosporium cladosporioides.

By modifying carbohydrate component of glycoproteins it is possible to elucidate its role in manifestation of structural and functional properties of the enzyme. The comparison of activity and stability of the native and modified by oxidation with sodium periodate α-galactosidase of Cladosporium cladosporioides was carried out. To determine α-galactosidase activity the authors used n-nitrophenyl synthetic substrate, as well as melibiose; raffinose and stachyose.

THERMAL STABILITY OF Cryptococcus albidus α-L-RHAMNOSIDASE.

Yeast as well as micromycetes α-L-rhamnosidases, currently, are the most promising group of enzymes. Improving of the thermal stability of the enzyme preparation are especially important studies. Increase in stability and efficiency of substrate hydrolysis by α-L-rhamnosidase will improve the production technology of juices and wines.

[OPTIMIZATION OF CULTIVATION CONDITIONS OF PENICILLIUM TARDUM--THE α-L- RHAMNOSIDASE PRODUCER].

The influence of some technological cultivation parameters of Penicillium tardum to synthesize of the extracellular α.-L-rhamnosidase were studied. It was shown that rhamnose (0.