Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
Compound
Query: EC:3.2.1.15 (
pectinase
)
2,440
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The enzymes used in the identification of Gram negative bacteria belonging to the families of Enterobacteriaceae, Vibrionaceae, Parvobacteriaceae, Pseudomonadaceae and to the genera Alteromonas, Xanthomonas, Alkaligenes, Flavobacterium are classified arbitrarily by the author into enzymes essential for the diagnosis of the family (oxidase, nitratase), enzymes useful in the diagnosis of the genus or the species (ONPG-hydrolase, urease, oxidative desaminase, lysine decarboxylase and ornithine, arginine dihydrolase, thiosulphate reductase,
pectinase
), and into enzymes sought to confirm the diagnosis (tetrathionate reductase, gelatinase, lipase, DNase, amylase,
beta-xylosidase
, lecithinase). The technics permitting their identification are described and their distribution in the species and genera studied is reported.
...
PMID:[Research technics of enzymes used in the diagnosis of gram negative bacteria (author's transl)]. 74 48
1. Polysaccharide depolymerases and glycoside hydrolases involved in the breakdown of plant structural polysaccharides (hemicellulose and pectins) were monitored in three fractions of the liquid phase of horse caecum digesta: acellular fluid (AF), bacteria (B) and protozoa plus bacteria (PB). 2. Both bacteria and protozoa were found to be involved in the decomposition of pectic substances, with two enzymic activities: depolymerase (
polygalacturonase
,
EC 3.2.1.15
; and pectin lyase, EC 4.2.2.10) and esterase (pectinesterase, EC 3.1.1.11). The activity of the PB fraction was higher than that of B. 3. With hemicellulosic substrates, all three fractions showed a significant xylan endo-1,3-beta-xylosidase (EC 3.2.1.32) activity. Mannan was hardly broken down. 4. Galactomannan and arabinogalactan were broken down more extensively by the PB fraction than by the B fraction. Glycosidase activities (
xylan 1,4-beta-xylosidase
,
EC 3.2.1.37
and alpha-L-arabinofuranosidase, EC 3.2.1.55) were also observed.
...
PMID:Degradation of hemicellulose and pectin by horse caecum contents. 340 1
The human colonic ecosystem is an extremely complex environment comprised of several hundred different strains of bacteria. Studies were undertaken to determine whether these organisms formed metabolic or genotypically distinct assemblages in the gut microbiota in relation to polysaccharide fermentation. Measurements of depolymerizing enzymes (4 polysac-charidases, 6 glycosidases) showed that specific amylase and
pectinase
activities were comparable in bacteria desorbed from the surfaces of food particles and in non-particulate organisms. However, xylanase,
beta-xylosidase
, arabinogalac-tanase, alpha-arabinofuranosidase, and beta-galacturonidase activities were always significantly greater in particulate bacteria. Short-term in vitro fermentations with both groups of bacteria showed marked differences in relative rates of starch, arabinogalactan, and mucin metabolism, while rates of fermentation product formation with pectin and xylan were broadly comparable. Significant differences were observed with respect to formation of individual fermentation products, especially when mucin or pectin were substrates, where particulate bacteria produced proportionally higher amounts of acetate. Bacteriological studies showed that communities of polymer-degrading bacteria and other groups of intestinal anaerobes growing on particulate matter were essentially similar to those occurring elsewhere in the gut lumen, at genus and species levels. In vitro colonization experiments demonstrated that a variety of polysaccharide-fermenting bifidobacteria and bacteroides--together with other cross-feeding organisms such as peptostreptococci, fusobacteria, and coliforms--rapidly attached to particulate intestinal materials.
...
PMID:Consequences of biofilm and sessile growth in the large intestine. 952 43
Apple-pectin hairy regions were prepared from apple pectin by combined action of the recombinant Aspergillus niger enzymes
endopolygalacturonase
II and pectin methylesterase and the A. tubigensis exopolygalacturonase. Using this enzymically prepared pectin fraction, an additional activity of the A. tubigensis exopolygalacturonase was discovered only when the substrate was chemically saponified and when D-galacturonate, a potent inhibitor of the enzyme, was removed from the incubation mixture. The new reaction product was purified and could be hydrolysed by A. niger
beta-xylosidase
into D-galacturonate and beta-D-xylose in a 1:1 ratio, which identified it as xylogalacturonate. The results demonstrate that exopolygalacturonase is not only active on galacturonan but also on xylogalacturonan. The enzyme thus accomodates a substrate in which the terminal galacturonic acid residue carries a single xylose substitution. The well-defined substrate specificity of exopolygalacturonase opens the possibility for use of this enzyme in biotechnological applications, such as preparing pectins that are methylated at the non-reducing end, and for studying the fine structure of xylogalacturonan in pectin.
...
PMID:The exopolygalacturonase from Aspergillus tubingensis is also active on xylogalacturonan. 1046 19
Xylanase, beta-glucosidase,
beta-xylosidase
, endoglucanase and
polygalacturonase
production from Curvularia inaequalis was carried out by means of solid-state and submerged fermentation using different carbon sources. beta-Glucosidase,
beta-xylosidase
,
polygalacturonase
and xylanase produced by the microorganisms were characterized. beta-Glucosidase presented optimum activity at pH 5.5 whereas xylanase,
polygalacturonase
and
beta-xylosidase
activities were optimal at pH 5.0. Maximal activity of beta-glucosidase was determined at 60 degrees C,
beta-xylosidase
at 70 degrees C, and
polygalacturonase
and xylanase at 55 degrees C. These enzymes were stable at acidic to neutral pH and at 40-45 degrees C. The crude enzyme solution was studied for the hydrolysis of agricultural residues.
...
PMID:Production, characterization and properties of polysaccharide depolymerizing enzymes from a strain of Curvularia inaequalis. 1183 Sep 41
Larval and adult Psacothea hilaris feed on mulberry wood and leaves, respectively. High levels of endogenous activity against the major dietary carbohydrates, cellulose, hemicellulose, starch and soluble sugars were secreted in the gut of larvae and adults. Activity against pectin was also high and multiple
polygalacturonase
(
EC 3.2.1.15
) components were secreted in the gut of larvae. One glycanase component, beta-EG1, which was primarily an endo-beta-1,4-glucanase (EC 3.2.1.4) and another, beta-EG2, which was mostly an endo-beta-1,4-xylanase (EC 3.2.1.8), were also secreted, while at least four additional components hydrolysed laminarin, lichenin and crystalline cellulose. The beta-glycosidase component beta-GD1 was associated with most of the beta-mannosidase (EC 3.2.1.25) and
beta-xylosidase
(
EC 3.2.1.37
) activity secreted in the gut of larvae, while another, beta-GD2, was a beta-glucosidase (EC 3.2.1.21), the activity of which was directed against cellobiose and other beta-linked disaccharides, and a beta-fucosidase (EC 3.2.1.38). A beta-galactosidase (EC 3.2.1.23), which did not hydrolyse lactose, was also secreted, as were distinct beta-N-acetylhexosaminidase (EC 3.2.1.52), trehalase (EC 3.2.1.28), alpha-L-arabinosidase (EC 3.2.1.55), alpha-galactosidase (EC 3.2.1.22) and a minimum of four alpha-glucosidase (EC 3.2.1.20) components, one of which was also likely to be associated with a peak of alpha-mannosidase (EC 3.2.1.24) activity. The alpha-glucosidase components varied in their specificity for alpha-linked disaccharides, but none was active against sucrose, which was hydrolysed by a beta-fructofuranosidase (EC 3.2.1.26) component. Overall average levels of activity in larvae were twice those of adults, but the secretion of individual carbohydrases in both was not regulated in response to the relative abundance of particular carbohydrate components in their respective diets.
...
PMID:Diet and carbohydrate digestion in the yellow-spotted longicorn beetle Psacothea hilaris. 1277 Apr 76
This paper reports the production of very high levels of cellulase free xylanase and associated hemicellulases by an indigenous thermophilic isolate of Thermomyces lanuginosus (D(2)W(3)) using solid-state fermentation. Sorghum straw, an inexpensive and abundant source of carbon supported maximal xylanase activity (11,855 units/g dry substrate). Culturing T. lanuginosus D(2)W(3) on sorghum straw and optimizing other culture conditions (media types, particle size of carbon source, inoculum level, inoculum age and additives), yielded increased levels of xylanase (39,726 units/g dry substrate). Further optimization of enzyme production was carried out using Box-Behnken design of experiments with three independent variables (inoculum level, glycerol and ammonium sulphate concentrations) which resulted in very high levels of xylanase, 48,000+/-1774 units/g dry substrate, and 2.6+/-0.2, 13.4+/-0.56, 68+/-1.7, 1.4+/-0.08, 1.2+/-0.05 (units/g dry substrate) of
beta-xylosidase
, alpha-galactosidase,
pectinase
, beta-mannosidase and alpha-L-arabinofuranosidase, respectively.
...
PMID:Sorghum straw for xylanase hyper-production by Thermomyces lanuginosus (D2W3) under solid-state fermentation. 1597 88
A method for analysis of the component composition of multienzyme complexes secreted by the filamentous fungus Trichoderma reesei was developed. The method is based on chromatofocusing followed by further identification of protein fractions according to their substrate specificity and molecular characteristics of the proteins. The method allows identifying practically all known cellulases and hemicellulases of T. reesei: endoglucanase I (EG I), EG II, EG III, cellobiohydrolase I (CBH I), CBH II, xylanase I (XYL I), XYL II,
beta-xylosidase
, alpha-L-arabinofuranosidase, acetyl xylan esterase, mannanase, alpha-galactosidase, xyloglucanase,
polygalacturonase
, and exo-beta-1,3-glucosidase. The component composition of several laboratory and commercial T. reesei preparations was studied and the content of the individual enzymes in these preparations was quantified. The influence of fermentation conditions on the component composition of secreted enzyme complexes was revealed. The characteristic features of enzyme preparations obtained in "cellulase" and "xylanase" fermentation conditions are shown.
...
PMID:New effective method for analysis of the component composition of enzyme complexes from Trichoderma reesei. 1603 8
The range of polysaccharide-degrading enzymes and glycosidases formed by the phytopathogenic fungus Sclerotinia sclerotiorum was monitored following growth on 16 carbohydrate substrates. Endo- and exoenzymes capable of degrading cellulosic, hemicellulosic, and pectinolytic polysaccharides were secreted. Pectinolytic activities were produced constitutively on all of the substrates tested. Cellulolytic enzymes were not induced in simple sugar (i.e., glucose or xylose) media. Polysaccharide growth substrates and cellulase inducers increased all of the enzyme activities tested. Gel filtration analysis revealed the appearance of new molecular forms of
pectinase
,
beta-xylosidase
, and cellobiosidase during induction on pectin and carboxymethyl cellulose media.
...
PMID:Production of Cell Wall-Degrading Enzymes by the Phytopathogenic Fungus Sclerotinia sclerotiorum. 1634 87
To investigate the role of ethylene in peach fruit softening during ripening, stony hard peach fruit, in which ethylene production is suppressed during ripening, were treated with various concentrations of ethylene. There was no noticeable decrease in flesh firmness without ethylene treatment, while applied ethylene, in the range 0.1-100 microl l(-1), resulted in fruit softening. Furthermore, the fruit softened more rapidly when the applied ethylene concentration was higher. When ethylene treatment was interrupted, the degree of softening was greatly reduced. These results indicated that continuous ethylene treatment was required for the initiation and progression of fruit softening and that ethylene concentration is also an important factor in regulating the rate of softening. Eight genes, which putatively encode cell wall metabolism-related proteins, were investigated for mRNA accumulation patterns in the two different softening phenotypes of melting and stony hard peaches. All of the mRNAs investigated accumulated in fruit of the melting-flesh "Akatsuki" during ripening. By contrast, in the stony hard-flesh "Manami", the mRNAs for a putative
endopolygalacturonase
(PpPG), an alpha-L-arabinofuranosidase/
beta-xylosidase
(PpARF/XYL), and an expansin (PpExp3) showed either much lower levels or did not accumulate, and were identified as softening-related genes. Interruption of ethylene treatment indicated that these genes were regulated at the transcriptional level, and quickly responded to the presence or absence of ethylene before the softening response occurred, suggesting that ethylene directly regulates the transcription of these softening-related genes. These results suggested that cell wall metabolism, causing a rapid loss of firmness in peach fruit, may be controlled by ethylene at the transcriptional level.
...
PMID:Ethylene-regulation of fruit softening and softening-related genes in peach. 1707 83
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