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)

The virus PBCV-1 attached rapidly, specifically, and irreversibly to the external surface of cell walls of its host, a unicellular, eukaryotic Chlorella-like green alga. Attachment was pH and salt dependent. Each cell contained at least 5 X 10(4) PBCV-1 binding sites and Scatchard analysis indicated that each cell could adsorb 5000 PBCV-1 particles. The PBCV-1 receptor was unaffected by extraction with organic solvents, detergents, high salts, or treatment with several proteases as well as the polysaccharide degrading enzymes, cellulase and pectinase. In contrast, acid and alkali treatments of walls at high temperatures and treatment with an enzyme preparation from PBCV-1 lysates destroyed the virus receptor. We suspect that the receptor is a carbohydrate.
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PMID:Properties of the Chlorella receptor for the virus PBCV-1. 336 63

Fermenting, pectolytic yeasts were isolated from a massive commercial outbreak of softening and gas-pocket formation in olives that had been stored in acidified, low-salt brines in an attempt to reduce the problem of brine disposal. The suspected yeasts represented three different species: Saccharomyces oleaginosus, S. kluyveri, and Hansenula anomala var. anomala. All pectolytic cultures produced pectin esterase and polygalacturonase but no pectic acid trans-eliminase when grown in nutrient glucose broth. Crude, cell-free dialyzed enzyme preparations measured viscosimetrically exhibited optimal activity on sodium polygalacturonate at pH 6.0 and 45 C and were active in the range of pH 4.0 to 9.0 and 10 to 60 C.
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PMID:Fermenting yeasts associated with softening and gas-pocket formation in olives. 501 77

A rapid and simple method was developed, using perfusion chromatography media, to separate the fruit-specific pectin methylesterase (PME) isoform from the depolymerizing enzyme polygalacturonase (PG) and other contaminating pectinases present in a commercial tomato enzyme preparation. Pectinase activities were adsorbed onto a Poros HS (a strong cation exchanger) column in 20 M HEPES buffer at pH 7.5. The fruit-specific PME was eluted from the column with 80 mM NaCl, followed by a step to 300 mM NaCl to elute PG activity. Rechromatography of the PME activity peak with a linear gradient further resolved two PME isoenzymes and removed residual traces of PG activity. The PG activity peak was further treated with lectin affinity chromatography to provide purified PG enzyme, which was separated from a salt-dependent PME (tentatively identified as a "ubiquitous-type" isoform), and a pectin acetylesterase. The later enzyme has not been reported previously in tomato. This method provides monocomponent enzymes that will be useful for studying enzyme mechanisms and for modifying pectin structure and functional properties.
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PMID:Perfusion chromatography separation of the tomato fruit-specific pectin methylesterase from a semipurified commercial enzyme preparation. 1151 90

Polygalacturonase isozyme 1 (PG1) is a heterodimer comprising a catalytic and noncatalytic or [beta] subunit, whereas polygalacturonase isozyme 2 (PG2) comprises only the catalytic subunit. To assess the state of assembly of PG1 in vivo, both subunits were purified to homogeneity and used to study assembly of the heterodimer. PG1 could be reconstituted in vitro from purified [beta] subunit and purified PG2 under a wide range of salt and pH conditions, and PG1 reconstituted in vitro was indistinguishable from PG1 isolated from tomato (Lycopersicon esculentum) fruit. Specific antibodies indicated that the [beta] subunit was present in fruit of all developmental stages, but absent in vegetative tissue. The state of assembly of PG1 in vivo was tested based on the differential thermal stability of PG1 and PG2 by heating segments of ripe fruit pericarp tissue. Temperatures well below those required to inactivate PG1 in vitro caused the loss of activity of both PG1 and PG2, suggesting that only heat-labile PG2 is present in vivo. In addition, when extracts of ripe fruit were rigorously maintained and analyzed at 4[deg]C, PG1 was absent or barely detectable. These results are consistent with the hypothesis that PG1 can assemble spontaneously and is essentially absent in intact tomato fruit but forms artifactually from PG2 and the [beta] subunit during the extraction of tomato fruit tissue when low temperatures are not rigorously maintained.
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PMID:Tomato Fruit Polygalacturonase Isozyme 1 (Characterization of the [beta] Subunit and Its State of Assembly in Vivo). 1223 22

Using anion-exchange chromatography on different carriers and phenyl-Sepharose hydrophobic chromatography, five pectolytic enzymes were isolated from the culture liquid of a mutant strain of Aspergillus japonicus: two endo-polygalacturonases (I and II, 38 and 65 kD, pI 5.6 and 3.3), pectin lyase (50 kD, pI 3.8), and two pectinesterases (I and II) with similar molecular weights (46 and 47 kD) and the same pI (3.8). The pectinesterases apparently represent two isoforms of the same enzyme. All purified enzymes were homogenous according to SDS-PAGE and polyacrylamide gel-IEF, except for endo-polygalacturonase II that gave two bands on isoelectric focusing, but one band on electrophoresis. All enzymes had maximal activity in an acid medium (at pH 4.0-5.5). The pectin lyase and pectinesterase were stable at 40-50 degrees C. The thermal stability of both endo-polygalacturonases was much lower (after 3 h of incubation at 30 degrees C, endo-polygalacturonases I and II lost 40 and 10% of the activity, respectively). The activity of endo-polygalacturonases I and II towards polygalacturonic acid strongly depended on NaCl concentration (optimal concentration of the salt was 0.1-0.2 M); the enzymes were also capable of reducing the viscosity of pectin solution, but rather slowly. The pectin lyase had no activity towards polygalacturonic acid. The activity of the pectin lyase increased with increasing degree of methylation of pectins. Both endo-polygalacturonases demonstrated synergism with the pectinesterase during the hydrolysis of highly methylated pectin. On the contrary, in the mixture of pectin lyase and pectinesterase an antagonism between the two enzymes was observed.
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PMID:Isolation and properties of pectinases from the fungus Aspergillus japonicus. 1288 38

The characterization of 23 Lactobacillus strains was performed. The strains were assayed for biogenic amine-forming capacity, hydrogen peroxide production, pectin esterase, cellulase and polygalacturonase production, growth rate, acidifying capacity and salt tolerance. Three strains were selected which belonged to the species, Lactobacillus brevis, Lactobacillus plantarum and Lactobacillus fermentum. Different starter cultures prepared as combinations of these three strains were assayed in pilot scale fermentations and Randomly Amplified Polymorphic DNA (RAPD) analysis, using a previously selected random primer, was applied for monitoring the inoculated strains. The course of fermentations was similar in all batches but sensorial analysis of eggplants fermented using a mixed culture of the three strains displayed the best results, and no differences were obtained when compared with commercial eggplants.
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PMID:Characterization of Lactobacillus strains and monitoring by RAPD-PCR in controlled fermentations of "Almagro" eggplants. 1597 83

Comparative analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of culture supernatants of a virulent Pseudomonas solanacearum strain and of a spontaneous avirulent mutant derived from it was performed. The results show that the levels of two major polypeptides with molecular masses of 43 and 25 kilodaltons (kDa) were markedly reduced in the spent culture medium of the avirulent mutant. In addition, enzyme assays showed that the level of carboxymethyl cellulase (endoglucanase) activity in the culture supernatants of the avirulent mutant was reduced over 25-fold, whereas polygalacturonase activities in both strains were nearly identical. Purification of the endoglucanase from the spent culture medium of the virulent P. solanacearum strain by adsorption to phosphocellulose, salt elution, and gel-filtration chromatography yielded a >95% pure preparation of the 43-kDa polypeptide. The kinetic and enzymatic properties of the purified endoglucanase were subsequently analyzed. Antibody prepared against the purified 43-kDa endoglucanase was used to demonstrate its production by several strains of P. solanacearum races 1 and 2.
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PMID:Purification and Characterization of an Endoglucanase from Pseudomonas solanacearum. 1634 43

Extracts from apple fruit (cultivar "Granny Smith") inhibited the cell-wall degrading polygalacturonase (PG) activity of Colletotrichum lupini, the causal agent of anthracnose on lupins, as well as Aspergillus niger PG. Southern blot analysis indicated that this cultivar of apple has a small gene family of polygalacturonase inhibiting proteins (pgips), and therefore heterologous expression in transgenic tobacco was used to identify the specific gene product responsible for the inhibitory activity. A previously isolated pgip gene, termed Mdpgip1, was introduced into tobacco (Nicotiana tabacum) by Agrobacterium-mediated transformation. The mature MdPGIP1 protein was purified to apparent homogeneity from tobacco leaves by high salt extraction, clarification by DEAE-Sepharose and cation exchange HPLC. Purified MdPGIP1 inhibited PGs from C. lupini and PGs from two economically important pathogens of apple trees, Botryosphaeria obtusa and Diaporthe ambigua. It did not inhibit the A. niger PG, which was in contrast to the apple fruit extract used in this study. We conclude that there are at least two active PGIPs expressed in apple, which differ in their charge properties and ability to inhibit A. niger PG.
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PMID:Apple polygalacturonase inhibiting protein1 expressed in transgenic tobacco inhibits polygalacturonases from fungal pathogens of apple and the anthracnose pathogen of lupins. 1636 81

Free protoplasts were prepared from the living bark tissue of the trunk of summer and winter black locust trees by enzymic digestion of thin slices of the tissue for 3 hours in a medium containing 2% Onozuka cellulase, 2% Rhozyme pectinase, and 2% Driselase in mannitol solutions using 0.4 molar mannitol for summer tissue and 1.0 molar mannitol for winter tissues. Cleaned suspensions of protoplasts and also thin slices of tissue with cells intact were frozen to temperatures of -10 C, -20 C, -30 C, -40 C and liquid nitrogen in sucrose and balanced salt solutions. Similar suspensions of protoplasts were also subjected to strong osmotic dehydration (plasmorrhysis) in a series of balanced salt solutions of increasing molarity. Tests for survival showed that protoplasts retain the same properties of either extreme susceptibility or extreme resistance to injury by freezing or osmotic dehydration as the cells from which they are prepared. Winter protoplasts showed capability for tolerating freezing to -196 C and plasmorrhysis in 5 molar salt solutions. These results indicate that protoplasts are a valid and useful system for investigating the properties of the protoplasm and surface membranes associated with the seasonal development of extreme hardiness in the cells of woody plants.
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PMID:Protoplasts surviving freezing to -196 C and osmotic dehydration in 5 molar salt solutions prepared from the bark of winter black locust trees. 1666 Aug

Tomato (Lycopersicon esculentum Mill) plants from various cultivars growing on half-strength Hoagland solution were exposed at anthesis to 3 or 6 grams per liter NaCl. Salinity shortened the time of fruit development by 4 to 15%. Fruits of salt-treated plants were smaller and tasted better than did fruits of control plants. This result was obtained both for ripe fruits tested on the day of picking and for those picked at 100% development and allowed to ripen at room temperature for 9 days. Percentage of dry weight, total soluble solids, and titratable acidity; content of reducing sugars, Cl(-), Na(+), and various pericarp pigments; and electrical conductivity of the juice were higher in fruits of saline-treated plants than they were in those of control plants, while the pH was lower. Ethylene and CO(2) evolution rates during ripening; as well as the activities of pectin methyl esterase, polymethylgalacturonase, and polygalacturonase; were also higher in fruits of the saline-treated plants. The treatment with 6 grams per liter NaCl shortened the fruit shelf life considerably.
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PMID:Effect of salinity on tomato fruit ripening. 1666 27


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