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 fungus Aspergillus terreus 17P--producer of cellulolytic enzymes--was cultivated in the Biotec 10 l fermenter on the medium containing minced and heated (at 200 degrees) wheat straw aerated with a different rate. At the mixing rate of 350 rpm and aeration rate of 0.7 r/rpm on the fourth day the culture liquid was obtained whose filtrate contained an active complex of cellulolytic enzymes and xylanase: CI--3.4; APB--1.1, Cx--35.7, cellobiase--0.23, xylanase--73.8 units/ml. The fractionation of the culture liquid filtrate with ammonium sulphate showed that the fraction precipitated at an interval of saturation of 0.3--0.7 contained the largest portion of cellulolytic enzymes and xylanase. The isolated enzymic preparations had a cellulolytic and xylanase activity and contained lipase, pectinase, laminarinase. They also contained low quantities of amylase, protease, beta-1,4- and beta-1,6-glucanase. Enzymic hylrolysis by the Asp. terreus 17P preparation of straw yielded glucose and xylose, of cotton, Na-KMC, cellobiose--glucose, Xylane hydrolyzate contained xylose and arabinose.
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PMID:[Biosynthesis of cellulolytic enzymes and xylanase during submerged cultivation of the fungus Aspergillus terreus 17P]. 10 86

The exudates or liquid droplets on various structures of a number of fungi were examined. The droplets were enveloped in membranous material and were associated with actively growing mycelia, including fruiting structures. Osmium tetroxide vapour-fixed droplets of Claviceps purpurea, Myrothecium roridum, Sclerotinia sclerotiorum, Sclerotium rolfsii, and Thanathephorus cucumeris did not dry to a powder but remained intact as spheres when freeze-dried. Fractured spheres, examined with the scanning electron microscope, showed the presence of a membranous structure similar to that of rapidly frozen colloidal solutions with the ice crystals removed by sublimation. Locules or cavities within the freeze-dried droplets are thought to be due to the entrapment of air when droplets coalesce. Biochemical analyses of the exudates showed that acid phosphatase, beta-glucosidase, acid and alkaline protease. RNase polygalacturonase and cellulase enzymes as well as oxalic acid and ammonia were present.
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PMID:Fungal exudates. 72 49

The various aspects of cellulose as a pollutant are considered in view of its lack of toxicity on the one hand and its recalcitrant durable nature on the other. The microbial degradation of cellulosics is discussed, and the contrast between its success in handling natural cellulosic wastes versus its failure to cope with man-made refuse is described. Research carried out in the past decade has demonstrated that cellulolytic organisms are provided with cell surface multifunctional multienzyme conglomerates, called cellulosomes, which are capable of solubilizing solid cellulosic substrates. The intriguing properties of such complexes include their cohesive nature, their many enzymatic components, and a characteristic glycosylated cellulose-binding, 'scaffolding' component. The latter appears to serve as a substrate-targeting carrier, which delivers the other (hydrolytic) components to the cellulose. Progress in establishing efficient model systems for in vitro solubilization of purified cellulose or natural cellulosic substrates has been achieved using purified cellulosome preparations, fortified with beta-glucosidase and pectinase. The latter enzymes were required in order to alleviate the phenomenon of product inhibition which reduces the efficiency of the free cellulosome. Such combined enzyme systems are proposed as examples of future tailor-made cellulolytic systems for the degradation of natural cellulosics.
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PMID:The cellulose paradox: pollutant par excellence and/or a reclaimable natural resource? 136 34

Peptide antibiotic AS-48 was purified to homogeneity by ion-exchange chromatography, gel filtration chromatography, and reversed-phase liquid chromatography. The purified fraction was active against gram-positive and gram-negative bacteria. AS-48 is a basic protein with an isoelectric point of ca. 10.5 and a molecular mass of 7.4 kilodaltons. Its inhibitory activity was markedly affected by sodium dodecyl sulfate and cardiolipin but not by neuraminidase, pectinase, beta-glucosidase, or beta-glucuronidase. Differential scanning calorimetry data suggested that AS-48 molecules lack a compact structure.
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PMID:Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48. 249 49

The pseudo-oligosaccharides, validamycins, showed potent inhibitory activity against trehalase of Rhizoctonia solani while no significant inhibition was exhibited against cellulase, pectinase, chitinase, alpha-amylase, alpha- and beta-glucosidases. In particular, validoxylamine A strongly inhibited trehalase in a competitive manner with a Ki value of 1.9 X 10(-9) M. The uptake of the antibiotic into the cell and the amount of the intracellular trehalose were investigated by incubating the washed mycelia of R. solani with validamycins. It was found that validamycin A is transported into the cell and hydrolyzed therein by a beta-glucosidase yielding validoxylamine A with greater inhibitory activity. Also validamycin A containing beta-D-glucosyl residue is more favorably taken up into the cell than validamycin D containing alpha-D-glucosyl residue or their common aglycone, validoxylamine A. In addition, validamycin A suppressed the in vivo degradation of the intracellular trehalose at very low concentration of 0.1 microgram/ml.
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PMID:Effect of validamycins on glycohydrolases of Rhizoctonia solani. 358 21

Activities of twelve hydrolytic enzymes in the digestive tract of young rabbits before weaning (4 weeks old) and adult rabbits (3 months old) were measured. The principal digestive enzymes in both groups of rabbits appeared to be amylase (EC 3.2.1.1), maltase (EC 3.2.1.20), pectinase (EC 3.2.1.15) and proteinases. The stomach of young rabbits contained most of the lipolytic activity and 45.7% of the total proteolytic activity of the digestive tract. The highest specific activities (per g digesta) of amylase, maltase and proteinase in young rabbits were found in the small intestine. Total activities (per segment) of amylase and maltase in the small intestine and the caecum were similar. Activities of cellulase (EC 3.2.1.4), inulinase (EC 3.2.1.7) and beta-glucosidase (EC 3.2.1.21) were low and activity of pectinase was fairly high in all segments of the digestive tract. The highest activity of urease (EC 3.5.1.5) was found in the caecum. Enzymic profiles of the colonic chymus resembled those of the caecum. Total hydrolytic activity was lower in the colon than in the caecum. Specific activities of amylase and invertase (EC 3.2.1.26) were lower and those of inulinase and lactase (EC 3.2.1.23) higher in 4-week-old rabbits than in 3-month-old rabbits. Gastric proteinase represented almost half of the total proteolytic activity of the digestive tract, whereas lipolytic activity of gastric contents was not found in measurable quantities in adult rabbits. The caecal contents of adult rabbits contained most of the total activity of lipase (EC 3.1.1.3), cellulase, xylanase (EC 3.2.1.32), pectinase, lactase, invertase, beta-glucosidase and urease present in the digestive tract.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Distribution of activity of hydrolytic enzymes in the digestive tract of rabbits. 753 89

A gene, CEL1, in the maize pathogen Cochliobolus carbonum was identified using the cbh1-3 gene of Phanerochaete chrysosporium as a heterologous probe. The predicted product of CEL1, Cel1, is 62% identical and 71% similar to the product of cbh1-3 and 54 to 62% identical to five cellobiohydrolases from other filamentous fungi. The location of the polyadenylation site 221 bp downstream of the stop codon and the location of a single intron of 55 bp were identified by comparison of the sequences of genomic and cDNA copies of CEL1. The transcriptional start site was determined by rapid amplification of cDNA ends (RACE) to be 39 bp upstream of the putative translational start site. CEL1 mRNA abundance is high when C. carbonum is grown on cellulose or maize cell walls but is undetectable when grown on 2% sucrose or cellulose plus sucrose. Cel1 has a predicted signal peptide of 18 amino acids and therefore a mature size of 46.4 kDa. Like the product of cbh1-1 of P. chrysosporium, but unlike most other endoglucanases and cellobiohydrolases (including the predicted product of cbh1-3), Cel1 does not have a putative cellulose binding domain or associated hinge region. The codon bias of CEL1 is stronger than the bias of cbh1-1 and comparable to that of cbh1-3 and that of the C. carbonum genes PGN1 and XYL1, (encoding endopolygalacturonase and endo-xylanase, respectively). A strain of C. carbonum specifically mutated at CEL1 was produced by transformation with a truncated copy of CEL1. Integration and disruption of CEL1 in the mutant was confirmed by DNA and RNA blotting. Pathogenicity of the CEL1 mutant was indistinguishable from the wild-type, indicating that CEL1 by itself is not a critical disease determinant. Culture filtrates of C. carbonum grown on cellulose or maize cell walls had several cellobiohydrolase, endoglucanase, and beta-glucosidase activities that were separable by chromatofocusing, hydrophobic interaction, or ion-exchange high-performance liquid chromatography.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region. 858 15

Pectin-rich residues from sugar beet processing contain significant carbohydrates and insignificant amounts of lignin. Beet pulp was evaluated for conversion to ethanol using recombinant bacteria as biocatalysts. Hydrolysis of pectin-rich residues followed by ethanolic fermentations by yeasts has not been productive because galacturonic acid and arabinose are not fermentable to ethanol by these organisms. The three recombinant bacteria evaluated in this study, Escherichia coli strain KO11, Klebsiella oxytoca strain P2, and Erwinia chrysanthemi EC 16 pLOI 555, ferment carbohydrates in beet pulp with varying efficiencies. E. coli KO11 is able to convert pure galacturonic acid to ethanol with minimal acetate production. Using an enzyme loading of 10.5 filter paper units of cellulase, 120.4 polygalacturonase units of pectinase, and 6.4 g of cellobiase (per gram of dry wt sugar beet pulp), with substrate addition after 24 h of fermentation, 40 g of ethanol/L was produced. Other recombinants exhibited lower ethanol yields with increases in acetate and succinate production.
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PMID:Fermentations of pectin-rich biomass with recombinant bacteria to produce fuel ethanol. 1084 85

Enzymatic activity of potential interest in wine-making was studied for 182 non-Saccharomyces yeasts isolated from musts before and at the onset of fermentation at wine cellars operating under the La Mancha Appellation of Origin in Spain. Tests were carried out on plates containing differential substrates appropriate for each case (casein, gelatin, polygalacturonic acid, and arbutin) to determine whether each of the isolates exhibited proteolytic, polygalacturonase, and beta-glucosidase activities. Nearly 80% of the wild yeasts possessed one or more enzymes of biotechnological interest. Once the enzymatic activities of the isolates had been established, 69 of the isolates that exhibited pronounced enzymatic activity and 11 randomly selected isolates that were devoid of any activity were typed using PCR/RFLP, which gave 13 different molecular profiles. The isolates for each of the profiles were then identified by classical methods. The enzyme beta-glucosidase was linked to the species Metschnikowia pulcherrima, and polygalacturonase activity was common in most of the species identified. Proteolytic activity was observed in Pichia membranifaciens and in Metschnikowia pulcherrima. Typing revealed the possibility of intraspecific differences in Pichia membranifaciens, because six different molecular profiles with one or more shared restriction bands were recorded for that species.
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PMID:Typing of non-Saccharomyces yeasts with enzymatic activities of interest in wine-making. 1094 36

Natural polysaccharides are now extensively used for the development of solid dosage forms for delivery of drug to the colon. The rationale for the development of a polysaccharide based delivery system for colon is the presence of large amounts of polysaccharidases in the human colon as the colon is inhabited by a large number and variety of bacteria which secrete many enzymes e.g. beta-D-glucosidase, beta-D-galactosidase, amylase, pectinase, xylanase, beta-D-xylosidase, dextranase, etc. Various major approaches utilizing polysaccharides for colon-specific delivery are fermentable coating of the drug core, embedding of the drug in biodegradable matrix, formulation of drug-saccharide conjugate (prodrugs). A large number of polysaccharides have already been studied for their potential as colon-specific drug carrier systems, such as chitosan, pectin, chondroitin sulphate, cyclodextrin, dextrans, guar gum, inulin, amylose and locust bean gum. Recent efforts and approaches exploiting these polysaccharides in colon-specific drug delivery are discussed.
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PMID:Polysaccharides in colon-specific drug delivery. 1147 12


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