Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.15 (pectinase)
2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protocol for isolating and regenerating protoplasts from Trichothecium roseum has been described. Protoplasts from T. roseum were isolated using (i) a lytic enzyme combination composed of Novozym 234, chitinase, cellulase, and pectinase at a 5-mg/mL concentration and (ii) 0.6 M KCl as an osmotic stabilizer. A maximum number of 28 x 10(4) protoplasts/mL were obtained at pH 5.5. Experiments on the regeneration and reversion of protoplasts revealed a maximum regeneration (60.8%) in complete medium (potato dextrose--yeast extract agar) amended with 0.6 M KCl. The regenerated protoplasts were similar to the original parent strain in morphology, pigmentation, growth, and sporulation.
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PMID:Release and regeneration of protoplasts from the fungus Trichothecium roseum. 1289 35

The influence of carbohydrates: glucose, fructose, galactose, galacturonic acid, xylose, lactose, sucrose, pectin and inulin, were evaluated as sole carbon source for the production of laccases by the ascomycete, Botryosphaeria sp. Veratryl alcohol, a laccase inducer, was added to culture media to study inducible laccase production on the same carbon sources. Inulinase and pectinase were also produced when Botryosphaeria sp. was grown on inulin, and galacturonic acid and pectin, respectively, and their levels were less in the presence of veratryl alcohol. Botryosphaeria sp. produced constitutive laccases on all carbon sources examined, and veratryl alcohol increased the laccase production on most of carbon sources studied except for inulin and galacturonic acid. Evidence is presented that Botryosphaeria sp. is also pectinolytic.
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PMID:The effect of carbohydrate carbon sources on the production of constitutive and inducible laccases by Botryosphaeria sp. 1296 81

A pectic polysaccharide named silenan, [alpha]D20 +148.6 degrees (c 0.1; H2O), was isolated earlier from the aerial part of campion, Silene vulgaris (Moench) Garcke. Silenan has been shown to contain homogalacturonan segments as "smooth regions" and rhamnogalacturonan fragments as "hairy regions". The present study reveals a generalization of structural features of silenan. Silenan was subjected to enzymic digestion with pectinase, to Smith degradation, and to lithium-degradation to determine the conforming poly- and oligosaccharide fragments of "hairy regions" of silenan. The NMR-spectral data and mass-spectrometry confirmed that the core of the ramified region of silenan consisted of residues of alpha-rhamnopyranose 2-O-glycosylated with the residues of alpha-1,4-D-galactopyranosyl uronic acid. The part of the alpha-rhamnopyranose residues of the backbone are branched at O-4. On the basis of the data, the hairy regions of silenan proved to contain mainly linear chains of beta-1,3-, beta-1,4-, and beta-1,6-galactopyranan and alpha-1,5-arabinofuranan. The side chains of the ramified region were shown to have branching points represented 2,3-, 3,6-, 4,6-di-O-substituted beta-galactopyranose residues.
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PMID:Structure of silenan, a pectic polysaccharide from Campion Silene vulgaris (Moench) Garcke. 1475 33

Arabidopsis thaliana mur1 is a dwarf mutant with altered cell-wall properties, in which l-fucose is partially replaced by l-galactose in the xyloglucan and glycoproteins. We found that the mur1 mutation also affects the primary structure of the pectic polysaccharide rhamnogalacturonan II (RG-II). In mur1 RG-II a non-reducing terminal 2- O-methyl l-galactosyl residue and a 3,4-linked l-galactosyl residue replace the non-reducing terminal 2- O-methyl l-fucosyl residue and the 3,4-linked l-fucosyl residue, respectively, that are present in wild-type RG-II. Furthermore, we found that a terminal non-reducing l-galactosyl residue, rather than the previously reported d-galactosyl residue, is present on the 2- O-methyl xylose-containing side chain of RG-II in both wild type and mur1 plants. Approximately 95% of the RG-II from wild type and mur1 plants is solubilized as a high-molecular-weight (>100 kDa) complex, by treating walls with aqueous potassium phosphate. The molecular mass of RG-II in this complex was reduced to 5-10 kDa by treatment with endopolygalacturonase, providing additional evidence that RG-II is covalently linked to homogalacturonan. The results of this study provide additional information on the structure of RG-II and the role of this pectic polysaccharide in the plant cell wall.
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PMID:l-Galactose replaces l-fucose in the pectic polysaccharide rhamnogalacturonan II synthesized by the l-fucose-deficient mur1 Arabidopsis mutant. 1499 5

Polygalacturonase inhibiting protein (PGIP) was extracted from 'Oroblanco' grapefruit type (triploid pummelo-grapefruit) albedo tissue, purified and partially characterized. Extraction was carried out at 4 degrees C with a high ionic strength extraction buffer. After dialysis and concentration by ultrafiltration the extract was chromatographed on concanavalin A-Sepharose. The PGIP activity was bound by the lectin and then eluted using 250 mM alpha-methyl mannopyranoside, resulting in a 17-fold purification of the PGIP and demonstrating its glycoprotein nature. The anion-exchange and size-exclusion chromatography steps that followed gave a PGIP that was 857-fold purified relative to the initial tissue extract, and having a 44 kDa molecular weight, as estimated by SDS-PAGE electrophoresis. PGIP inhibition activity was tested with endo-polygalacturonase (EC 3.2.1.15) produced by Penicillium italicum and Botrytis cinerea. The radial diffusion and reducing sugar assays showed that P. italicum and B. cinerea endo-PGs were affected by PGIP, whereas no endo-PG activity was detected in the culture filtrate of P. digitatum. In vitro tests revealed that PGIP inhibited P. italicum and B. cinerea growth. By contrast, the influence of PGIP on P. digitatum, growth was negligible, perhaps because this fungus does not produce endo-PG. Following heating for 10 min at 65 degrees C the inhibitory activity of PGIP was reduced by 43%. PGIP activity decreased further as heating temperature increased, and was completely suppressed after heating at 100 degrees C for 10 min.
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PMID:Properties of a polygalacturonase-inhibiting protein isolated from 'Oroblanco' grapefruit. 1503 36

Eight wine yeast strains of Saccharomyces sp. were tested for polygalacturonase (PGase) activity, after cultivation on various carbon sources. No strain showed any activity when grown on glucose, while five strains produced PGase in the presence of galactose and polygalacturonate. These data suggest that the PGase of wine strains is repressed by glucose and induced by galactose and polygalacturonate. The existence of the PGase gene in the wine strains and its similarity with that of the laboratory strains was proved by Southern hybridization and PCR amplification. The promoter region of the PGase gene in the wine strains was slightly different from that of the laboratory strains. This possibly explains the different pattern of gene expression in wine and laboratory strains. The PGase of wine strains produced di- or tri-galacturonic acid from polygalacturonic acid, different from the fungal PGase.
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PMID:Endo-polygalacturonase in Saccharomyces wine yeasts: effect of carbon source on enzyme production. 1578 Jun 66

Pectin with [alpha]D(20) +192 degrees (c 0.1; water), named comaruman, was isolated from marsh cinquefoil Comarum palustre L., which is widespread in the European North. The sugar chain of comaruman contains residues of D-galacturonic acid (64%), D-galactose (13%), L-rhamnose (12%), L-arabinose (6%), and trace amounts of xylose and glucose. Partial acid hydrolysis and digestion with pectinase demonstrated that comaruman composed of the backbone comprised regions of linear alpha-1,4-D-galactopyranosyl uronan interconnected by numerous residues of alpha-1,2-L-rhamnopyranose. In addition to the backbone (core of the macromolecule), ramified regions are involved in comaruman and comprise alpha-2,4-L-rhamno-alpha-4-D-galacturonan with side chains consisting mainly of beta-1,4-linked residues of D-galactopyranose. The ramified region contains additionally residues of 5-O-substituted arabinofuranose and 3- and 6-O-substituted galactopyranose. The present 3,4- and 4,6-di-O-substituted residues of galactopyranose appear to be branching points of the side chains. Some galactopyranose residues were found to occupy the terminal positions of the side chains or appeared to be single sugar residues attached to the side chains. Methylation analysis data indicated that comaruman contains residues of terminal, 3- and 3,4-di-O-substituted galactopyranosyl uronic acid, which appeared to be constituents of the side chains, and the latter represented additionally branching points of the backbone.
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PMID:Structural studies on pectin from marsh cinquefoil Comarum palustre L. 1621 42

The body complex of the soybean seed (BCSS) was isolated from the single cells (27.2%) by a sequential procedure of autoclaving with water, cellulase digestion for the primary cell wall, pectinase digestion for the secondary cell wall, and defatting with hexane washing. Its characteristics were then investigated. The defatted BCSS (DBCSS) consisted of protein (76.5%) and mannose-rich carbohydrates (3.2%). Screening of the food-processing protease for the digestion of DBCSS was carried out, and a kind of alkaline protease was selected. The inner protein of DBCSS was easily extracted with 0.1 M sodium carbonate buffer, pH 10, and the insoluble shell of the body complex (SDBCSS) was left. SDBCSS consisted of hydrophobic amino acid-rich protein. SDBCSS was easily digested by the selected alkaline protease. SDBCSS was dissolved by boiling with sodium dodecyl sulfate-mercaptoethanol, and it was found to consist of a protein of approximately 3 kDa. The high enzymatic digestion including the selected protease for soybean seed and defatted soybean meal was carried out; both were extracted and digested with a yield of >99.5%. The final indigestible residue was found as paired hexagonal and filamentous organs of the soybean cells.
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PMID:Isolation and enzymatic digestion of body complex of soybean seed. 1636 90

The Ordos Plateau in China is covered with up to 300,000 ha of peashrub (Caragana) which is the dominant natural vegetation and ideal for fodder production. To exploit peashrub fodder, it is crucially important to optimize the culture conditions, especially culture substrate to produce pectinase complex. In this study, a new prescription process was developed. The process, based on a uniform experimental design, first optimizes the solid substrate and second, after incubation, applies two different temperature treatments (30 degrees C for the first 30 h and 23 degrees C for the second 42 h) in the fermentation process. A multivariate regression analysis is applied to a number of independent variables (water, wheat bran, rice dextrose, ammonium sulfate, and Tween 80) to develop a predictive model of pectinase activity. A second-degree polynomial model is developed which accounts for an excellent proportion of the explained variation (R(2)=97.7%). Using unconstrained mathematical programming, an optimized substrate prescription for pectinase production is subsequently developed. The mathematical analysis revealed that the optimal formula for pectinase production from Aspergillus niger by solid fermentation under the conditions of natural aeration, natural substrate pH (about 6.5), and environmental humidity of 60% is rice dextrose 8%, wheat bran 24%, ammonium sulfate ((NH(4))(2)SO(4)) 6%, and water 61%. Tween 80 was found to have a negative effect on the production of pectinase in solid substrate. With this substrate prescription, pectinase produced by solid fermentation of A. niger reached 36.3 IU/(gDM). Goats fed on the pectinase complex obtain an incremental increase of 0.47 kg day(-1) during the initial 25 days of feeding, which is a very promising new feeding prospect for the local peashrub. It is concluded that the new formula may be very useful for the sustainable development of arid and semiarid pastures such as those of the Ordos Plateau.
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PMID:Pectinase production by solid fermentation from Aspergillus niger by a new prescription experiment. 1640 99

Previous studies have revealed the inhibitory effects of an acidic polysaccharide purified from the root of Panax ginseng against the adhesion of Helicobacter pylori to gastric epithelial cells and the ability of Porphyromonas gingivalis to agglutinate erythrocytes. In this study, this acidic polysaccharide from P. ginseng, PG-F2, was investigated further, in order to characterize its antiadhesive effects against Actinobacillus actinomycetemcomitans, Propionibacterium acnes, and Staphylococcus aureus. The minimum inhibitory concentrations (MIC) were found to be in a range of 0.25-0.5mg/mL. However, results showed no inhibitory effects of PG-F2 against Lactobacillus acidophilus, Escherichia coli, or Staphylococcus epidermidis. PG-F2 is a pectin-type polysaccharide with a mean MW of 1.2 x 10(4) Da, and consists primarily of galacturonic and glucuronic acids along with rhamnose, arabinose, and galactose as minor components. The complete hydrolysis of PG-F2 via chemical or carbohydrolase enzyme treatment resulted in the abrogation of its antiadhesive activity, but limited hydrolysis via treatment with pectinase (EC. 3.2.1.15) yielded an oligosaccharide fraction, with activity comparable to the precursor PG-F2 (the MIC of ca. 0.01 mg/mL against H. pylori and P. gingivalis). Our results suggest that PG-F2 may exert a selective antiadhesive effect against pathogenic bacteria, while having no effects on beneficial and commensal bacteria.
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PMID:Pectin-like acidic polysaccharide from Panax ginseng with selective antiadhesive activity against pathogenic bacteria. 1664 69


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