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)

UV-C irradiation (254 nm) was found to enhance the secretion of some cell-wall-degrading enzymes, especially the following carbohydrases: beta-galactosidase, alpha-L-arabinofuranosidase, polygalacturonase, pectinesterase, cellulase, xylanase, and beta-xylosidase, in the campion callus, contributing thereby to an alteration in the polysaccharide structure. The relative amounts of the galactose and arabinose residues in pectin (silenan) and of arabinose in arabinogalactan of calli irradiated during the exponential phase were shown to decrease during the stationary phase. A decrease in the degree of SV methylesterification was found for the irradiated callus. These alterations were found to persist over a long period of culturing time. Decreasing the relative amounts of the arabinose residues in arabinogalactan and pectin and the galactose residues in silenan corresponded to increasing activity of alpha-L-arabinofuranosidase and beta-galactosidase, respectively, due to treatment with UV-C. UV-C irradiation may be used as a tool for modifying the structural features of the cell-wall polysaccharides, such as the relative amounts of galactose and arabinose residues in the side chains of polysaccharides, with the purpose of obtaining physiologically active polysaccharides with the desired properties and structural features.
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PMID:Influence of ultraviolet-C on the compositions of cell-wall polysaccharides and carbohydrase activities of Silene vulgaris callus. 1718 64

A pectolytic enzyme preparation from Aspergillus niger (pectinase AN) decreased most rutin content and antioxidant activity of asparagus juice. To investigate the mechanism of such loss, we analyzed several possible related enzyme activities in pectinase AN. We found that the activity of pectinase AN to oxidize guaiacol had no significant difference with or without the presence of H2O2; thus it was laccase activity, not peroxidase (PO) activity, that pectinase AN contained. We did not find any polyphenol oxidase (PPO) activity in pectinase AN. Laccase in pectinase AN could be the major cause of loss of rutin and antioxidant activity of asparagus juice. When most laccase activity of pectinase AN was inactivated after heating at 70 degrees C for 1.5 min and incubated with asparagus juice, the loss rate of rutin was only 9% of that treated with unheated pectinase AN, and the antioxidant activity was even increased. Rhamnosidase activity was detected in pectinase AN and can change rutin in asparagus juice to quercetin-3-glucoside, which has higher antioxidant activity than rutin. This may explain the increase of antioxidant activity of asparagus juice treated with heated pectinase AN that still contained some rhamnosidase activity. The discovery of our research is helpful to produce juice with high antioxidant activity and high health benefits in the juice industry.
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PMID:Enzyme-catalyzed change of antioxidants content and antioxidant activity of asparagus juice. 1719 13

The rough lemon (Citrus jambhiri) gene encoding polygalacturonase-inhibiting protein (RlemPGIPA) was overexpressed in the pathogenic fungus Alternaria citri. The overexpression mutant AcOPI6 retained the ability to utilize pectin as a sole carbon source, and the overexpression of polygalacturonase-inhibiting protein did not have any effect on the growth of AcOPI6 in potato dextrose and pectin medium. The pathogenicity of AcOPI6 to cause a black rot symptom in citrus fruits was also unchanged. Polygalacturonase-inhibiting protein was secreted together with endopolygalacturonase into culture filtrates of AcOPI6, and oligogalacturonides were digested from polygalacturonic acid by both proteins in the culture filtrates. The reaction mixture containing oligogalacturonides possessed activity for induction of defense-related gene, RlemLOX, in rough lemon leaves.
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PMID:Overexpression of citrus polygalacturonase-inhibiting protein in citrus black rot pathogen Alternaria citri. 1722 23

During bell pepper (Capsicum annuum L.) fruit ripening, beta-galactosidase activity increased markedly as compared with other glycosidases. We purified 77.5 kDa exo-1,4-beta-D-galactanase from red bell pepper fruit classified as beta-galactosidase II. A marked decrease in galactose content appeared during fruit ripening, especially in the pectic fraction. The purified enzyme hydrolyzed a considerable amount of galactose residues in this fraction. We isolated bell pepper beta-galactosidase (PBG1) cDNA. This PBG1 protein contained the putative active site, G-G-P-[LIVM]-x-Q-x-E-N-E-[FY], belonging to glycosyl hydrolase family 35. Quantitative RT-PCR revealed that the expression of PBG1 in red fruit was significantly stronger than that from any other tissues. Moreover, expression of PBG1 occurred prior to that of pepper endo-polygalacturonase 1 (PPG1), the major fruit-ripening enzyme. Based on these results, it appears that the hydrolysis of galactose residues in pectic substances is the first event in the ripening process in bell pepper fruit.
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PMID:Pepper beta-galactosidase 1 (PBG1) plays a significant role in fruit ripening in bell pepper (Capsicum annuum). 1728 22

A pectin polysaccharide named bergenan was isolated from the freshly collected leaves of the leather bergenia Bergenia crassifolia by extraction with an aqueous solution of ammonium oxalate. The main component of its carbohydrate chain was shown to be the residues of D-galacturonic acid (about 80%). In addition, the polysaccharide contains residues of galactose, arabinose, and rhamnose; their total content is less than 15%. It was shown that the bergenan samples from bergenia leaves collected at different vegetation periods (from July to September) do not substantially differ either in monosaccharide composition or in the viscosity of aqueous solutions they form. The results of enzymatic hydrolysis by alpha-1,4-galacturonase (pectinase), partial acidic hydrolysis, NMR spectroscopy, and methylation with subsequent analysis of the results by GC-MS indicate that the bergenan macromolecule contains the regions of a linear alpha--1,4-D-galactopyranosyluronan and rhamnogalacturonan-I (RG-1). Galacturonan responds for a greater part of the macromolecule. A considerable amount of its constituent galacturonic acid residues are present as methyl esters. The side chains in RG-I are attached to the rhamnopyranose residues of the main carbohydrate chain by 1,4-link and are composed of the residues of terminal arabinofuranose and galactopyranose, 1,5-linked (-arabinofuranose, and 1,4-and 1,6-linked beta-galactopyranose. The branching points of the side chains of the RG-I molecule are 3,4- and 3,6-di-O-substituted galactose residues.
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PMID:[Structural study of bergenan, a pectin from Bergenia crassifolia]. 1737 59

The aim of this paper was to further elucidate the structure and the immunomodulating properties of the pectic polymer GOA2, previously isolated from Glinus oppositifolius. Enzymatic treatment of GOA2 by endo-alpha-d-(1 --> 4)-polygalacturonase led to the isolation of three pectic subunits, GOA2-I, GOA2-II, and GOA2-III, in addition to oligogalacturonides. GOA2-I was shown to consist of 1,2-linked Rhap and 1,4-linked GalpA in an approximately 1:1 ratio, and NMR-analysis showed that the monomers were linked together in a strictly alternating manner. The galactose units in GOA2-I were found as terminal-, 1,3-, 1,6-, 1,4-, 1,3,4-, and 1,3,6-linked residues, while the arabinofuranosyl existed mainly as terminal- and 1,5-linked units. A rhamnogalacturonan-I type structure was suggested being the predominant part of GOA2-I. According to linkage analysis GOA2-II and GOA2-III contained glycosidic linkages characteristic for rhamnogalacturonan-II type structures. GOA2 was shown by sedimentation velocity in the analytical ultracentrifuge, to have a broad degree of polydispersity with a mode s(20,w) value of approximately 1.9 S, results reinforced by atomic force microscopy measurements. The polydispersity, as manifested by the proportion of material with s(20,w) > 3 S, decreased significantly with enzyme treatment. The abilities of GOA2, GOA2-I, GOA2-II, and GOA2-III to induce the proliferation of B cells, and to exhibit complement fixing activities were tested. In both test systems, GOA2-I showed significantly greater effects compared to its native pectin GOA2. GOA2-I was in addition shown to exhibit a more potent intestinal immune stimulating activity compared to GOA2. The ability of GOA2 to induce secretion of proinflammatory cytokines was examined. Marked upregulations in mRNA for IL-1beta from rat macrophages and IFN-gamma from NK cells were found.
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PMID:Immunological and structural properties of a pectic polymer from Glinus oppositifolius. 1772 87

Polysaccharides (pectin and intracellular and extracellular arabinogalactans) were isolated from campion callus culture cultivated on medium with varied concentrations of pectinase and beta-galactosidase. A decrease in contents of arabinose residues in pectin and arabinogalactans and of galactose residues in arabinogalactans was associated with an increase in the activities of alpha-L-arabinofuranosidase and beta-galactosidase upon addition of pectinase into the medium. Pectinase destroyed the high-molecular-weight (more than 300 kD) fraction of pectin and decreased the content of galacturonic acid residues. alpha-L-Arabinofuranosidase transformed arabinogalactan into galactan, and galactan was destroyed under the influence of galactosidase. The contents of arabinogalactan and/or galactan in the cells were decreased, and it was released into the culture medium. Pectin samples with low contents of arabinose and galactose in the side chains and galactan samples were obtained from the callus grown on the medium with beta-galactosidase. Cultivation of the plant cells on medium containing carbohydrases resulted in modification of pectin and arabinogalactan of the cell walls.
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PMID:Modification of polysaccharides from callus culture of Silene vulgaris (M.) G. using carbohydrases in vitro. 1792 61

After observing the effects of purified cellulase (C), hemicellulase (H), pectinase (P), and their combinations on the in vitro digestibility of a corn-soybean meal broiler diet, we examined the associations between pectin breakdown and the digestibilities of CP and DM by using free galacturonic acid (GA) as an index of pectin breakdown. There was no significant effect of the single enzymes except for H. However, the enzyme combinations H + P, C + H, and C + H + P significantly increased CP and DM digestibilities, whereas the combination of C + P was not effective. Because H has activities of both H and P, these enzymes were considered to be important in stimulating digestion. Furthermore, when the enzymes increased CP and DM digestibilities, GA concentration was significantly higher, and clear correlations between CP and DM digestibilities and GA concentration were observed, whereas correlations between the digestibilities and concentration of glucose or xylose + mannose as indices of cellulose and hemicellulose breakdown, respectively, were not significant. From these observations, we hypothesized that a mixture of enzymes could increase the protein digestibility of broiler feed. Thus, in the in vivo experiment, low-protein (19% CP) diets made mainly of corn and soybean meal with or without mixed enzymes were prepared and given to broiler chicks. The birds given the diet containing mixed enzymes showed significantly higher BW gain, with higher CP and DM digestibilities than the birds given the diet without the mixed enzymes. Moreover, the growth rate was same as that of the birds given the normal (21% CP) diet. The results indicate that the mixed enzyme preparation can effectively degrade indigestible cell constituents and thus enable the protein of the broiler feed to become more digestible. Furthermore, the results indicate the importance of H as a rate-limiting factor of cell wall breakdown.
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PMID:An effective combination of carbohydrases that enables reduction of dietary protein in broilers: importance of hemicellulase. 1833 93

An alkali extract of cell walls of Gossypium hirsutum L. was sequentially digested by endo-polygalacturonase (EC 3.2.1.15), arabinofuranosidase AN1571.2 (EC 3.2.1.55), endo-arabinase (EC 3.2.1.99), and rhamnogalacturonan hydrolase AN9314.2 (EC 3.2.1.15). The rhamnogalacturonan hydrolase-generated oligosaccharides were separated by ultrafiltration, size-exclusion, and anion exchange chromatography. Fractions from the anion exchange chromatography were pooled, lyophilized, and screened by MALDI-TOFMS. A new oligosaccharide (RGS29), which contained a rhamnogalacturonan dimer backbone with two galactose and two arabinose residues in the side chains, was found. Its structure was identified by 1D and 2D NMR spectra as follows: [Formula: see text].
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PMID:Isolation and structural characterization of a novel oligosaccharide from the rhamnogalacturonan of Gossypium hirsutum L. 1835 94

A washed carrot substrate, prepared with high yields and easy handling properties, was found to be a suitable substrate for studying cellulolytic and pectinolytic degradation processes. A cellulase from Trichoderma reesei, and Rohament P, a macerating enzyme from Aspergillus alleaceus in endopolygalacturonase, degraded the washed carrot substrate to an extent of 60%. With the combined action of both enzymes, degradation was more than 80%. Simultaneous action of both enzymes was more efficient than their sequential use. The effect of temperature, pH, incubation time, enzyme concentration, and substrate concentration on the degradation by the single enzymes and their mixture were studied. Gas chromatographic sugar analysis revealed that Rohament P liberated glucose, arabinose, and galactose in the low-molecular-weight fraction obtained by ultrafiltration, in addition to high amounts of galacturonic acid. These carbohydrates were also found in the high-molecular-weight fraction (retentate) together with rhamnose and mannose. Cellulase BC released mainly glucose, although galacturonic acid, arabinose, xylose, and mannose were also detected both in the ultrafiltrate and retentate. Morphologically, during Rohament P degradation of the washed carrot substrate, damaged tissues and disintegrated cells were seen, whereas on cellulase BC action mainly disintegrated cell walls were observed.
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PMID:Degradation of a washed carrot preparation by cellulases and pectinases. 1855 48


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