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At least 19 recordsLinked to original sources
PubMed1991

Synthesis of different pectinases by filamentous growing A. niger mutants.

Mutants of A. niger K 69/26, prepared by multistep mutagenesis (UV, MNNG, heating) have been screened for pectinase activities. Mutants with altered levels of certain pectinases, such as endo- and exopolygalacturonase (PG vis, red), pectinesterase (PE) and pectinlyase (PL), were isolated. The enzyme activities of the best mutants M 1348/126 were increased 2-3-fold compared to the parent strain after a 6-d cultivation of filamentous mycelium on a shaker. Further mutagenesis of mutants with decreased pectinase activities (e.g. Se3) produced revertants. PG (vis) synthesis of revertant Se5 was increased 1.7 times compared to the control strain K 69/26. Independent of these increased rates, the general level of pectinase activities synthesized by the filamentous mycelium of A. niger mutants amounts to about 10-20% compared with those produced by aggregated mycelium. It appears that the enzyme synthesis related to mycelium structure is independent of the mechanism which regulates the level of pectinase synthesis within a specific morphological structure.

Aspergillus niger↗
PubMed1992

Environmental conditions affect transcription of the pectinase genes of Erwinia chrysanthemi 3937.

To depolymerize plant pectin, the phytopathogenic enterobacterium Erwinia chrysanthemi produces a series of enzymes which include a pectin-methyl-esterase encoded by the pem gene and five isoenzymes of pectate lyases encoded by the five genes pelA, pelB, pelC, pelD, and pelE. We have constructed transcriptional fusions between the pectinase gene promoters and the uidA gene, encoding beta-glucuronidase, to study the regulation of these E. chrysanthemi pectinase genes individually. The transcription of the pectinase genes is dependent on many environmental conditions. All the fusions were induced by pectic catabolic products and responded, to different degrees, to growth phase, catabolite repression, temperature, and nitrogen starvation. Transcription of pelA, pelD, and pelE was also increased in anaerobic growth conditions. High osmolarity of the culture medium increased expression of pelE but decreased that of pelD; the other pectinase genes were not affected. The level of expression of each gene was different. Transcription of pelA was very low under all growth conditions. The expression of the pelB, pelC, and pem genes was intermediate. The pelE gene had a high basal level of expression. Expression of pelD was generally the most affected by changes in culture conditions and showed a low basal level but very high induced levels. These differences in the expression of the pectinase genes of E. chrysanthemi 3937 presumably reflect their role during infection of plants, because the degradation of pectic polymers of the plant cell walls is the main determinant of tissue maceration caused by soft rot erwiniae.

Anaerobiosis↗
PubMed2026

Scalable production of pectinases from Bacillus licheniformis SMIA-2 using agro-Industrial by-products with genomic insights.

UNLABELLED: The study re-analyzed the draft genome of Bacillus licheniformis SMIA-2 and generated a reference-guided pseudo-scaffold. Cross-validated genome annotation identified five candidate loci associated with pectin degradation, including putative pectate lyases, polygalacturonase, and downstream uronate-catabolic genes. Submerged fermentation with passion fruit peel flour and corn steep liquor yielded crude enzymatic extracts, which were spray-dried at 110 °C using maltodextrin and microcrystalline cellulose as stabilizers. The dried formulation retained pectinase activity for 180 days at 5 °C and showed additional cellulase, amylase, xylanase, and protease activities. Pectinase displayed optimal activity at pH 8.5 and 70 °C, with stability between pH 8.0-8.5 and 65-70 °C. Despite not using a reference strain and the absence of some omics analyses, with genomic and industrial claims presented as evidence of biotechnological potential rather than definitive functional validation of individual genes, these results support a sustainable, scalable, and alkaline-tolerant enzyme platform based on agro-industrial residues. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at https://doi.org/10.1007/s10068-026-02252-3.

Agro-industrial residues↗
PubMedDate not supplied

Use of pectinases complexed to colloidal gold for the ultrastructural localization of polygalacturonic acids in the cell walls of the fungus Ascocalyx abietina.

Three pectinase--gold complexes were used to localize polygalacturonic acids in the fungus Ascocalyx abietina (Lagerberg) Schlaepfer-Bernhard. With the pectinesterase and pectin lyase--gold complexes, the labelling was uniformly distributed over the fungus walls and did not seem to be significantly influenced by the tissue preparation. With the polygalacturonase--gold complex, differences in the labelling distribution were noted according to the fixation procedure indicating, therefore, that osmication of the tissues could greatly interfere with the localization of the specific enzyme binding sites. These results demonstrate, for the first time, the possibility of detecting polygalacturonic acids by means of different gold-complexed pectinases.

Ascomycota↗
PubMed1985

New matrices for the purification of pectinases by affinity chromatography.

Polygalacturonic acid was used as a ligand in the affinity technique for pectinases purification from the filtrate of Aspergillus niger 71 culture. For this purpose four matrices were examined, namely, alkylamine controlled porous glass (CPG), alkylamine silica gel as well as keratin or polyamide coated silica gel. Good results of pectinase purification was obtained on silanized CPG or keratin coated silica gel supports.

Amines↗
PubMed1989

A reappraisal of the terverticillate penicillia using biochemical, physiological and morphological features. III. An evaluation of pectinase and amylase isoenzymes for species characterization.

Polyacrylamide gel electrophoresis of extracellular pectinase and amylase isozymes of 170 mainly terverticillate Penicillium strains was undertaken. The data were coded and subjected to numerical analysis. Variation in intensity of isozymes was observed in repeat analyses of some strains, although most were consistent. Variation was also observed between some representative strains of species. P. viridicatum was more variable than P. brevicompactum and P. hordei for intensity of pectinase activity. There was a correlation between the grouping of the strains on the basis of the isozymes and the species concepts only in some cases. The method proved useful for the identification of strains producing intense activity which provided clear patterns, for example, P. brevicompactum and P. chrysogenum and to a lesser extent P. solitum var. crustosum and P. hordei. The method was also exclusionary in that some species were restricted to a particular cluster or subcluster. Amylase patterns confirmed that strains referred to as single species are not all homogeneous genetically, and that some strains are not simply haploid homokaryons. The genetic heterogeneity of the strains explains some of the problems in the systematics of the terverticillate penicillia.

Amylases↗
PubMed1991

Pectinase production by Neurospora crassa: purification and biochemical characterization of extracellular polygalacturonase activity.

The production of pectinase was studied in Neurospora crassa, using the hyperproducer mutant exo-1, which synthesized and secreted five to six times more enzyme than the wild-type. Polygalacturonase, pectin lyase and pectate lyase were induced by pectin, and this induction was glucose-repressible. Polygalacturonase was induced by galactose four times more efficiently than by pectin; in contrast the activity of lyases was not affected by galactose. The inducing effect of galactose on polygalacturonase was not glucose-repressible. Extracellular pectinases were separated by ion exchange chromatography. Pectate and pectin lyases eluted into three main fractions containing both activities; polygalacturonase eluted as a single, symmetrical peak, apparently free of other protein contaminants, and was purified 56-fold. The purified polygalacturonase was a monomeric glycoprotein (38% carbohydrate content) of apparent molecular mass 36.6-37.0 kDa (Sephadex G-100 and urea-SDS-PAGE, respectively). The enzyme hydrolysed predominantly polypectate. Pectin was also hydrolysed, but at 7% of the rate for polypectate. Km and Vmax for polypectate hydrolysis were 5.0 mg ml-1 and 357 mumol min-1 (mg protein)-1, respectively. Temperature and pH optima were 45 degrees C and 6.0, respectively. The purified polygalacturonase reduced the viscosity of a sodium polypectate solution by 50% with an increase of 7% in reducing sugar groups. The products of hydrolysis at initial reaction times consisted of oligogalacturonates without detectable monomer. Thus, the purified Neurospora crassa enzyme was classified as an endopolygalacturonase [poly(1,4-alpha-D-galacturonide) glycanohydrolase; EC 3.2.1.15].

Chromatography↗
PubMed1979

Feulgen cytophotometry of pine nuclei. II. Effect of pectinase used in cell separation.

Pectinase used for cell separation prior to cytophotometry contains a DNase that is able to penetrate the cells of pine root tips and attack nuclear DNA. When pine root tips were exposed to 1% pectinase (pH 6.0), there was a decrease in nuclear DNA content at every sample point and a sharp drop between 16 and 20 hr. The effect of the DNase was eliminated by preparing the enzyme solution in 0.01 M sodium citrate or 0.001 M EDTA. It is suggested that heat denaturation of the DNase should also be effective and might be used in combination with the magnesium chelators.

Cell Separation↗
PubMed1985

Plate assay for determining the time of production of protease, cellulase, and pectinases by germinating fungal spores.

A new method for detecting enzymes produced by fungal spores during germination is described here. With this method, the production of enzymes such as protease, cellulase, or pectinase can be correlated with the extent of spore germination. Germination is studied in vitro on agar-based media containing protein, cellulose, or pectin. The spores are immobilized on a permeable membrane mounted on the substrate-containing medium. At various times after inoculation the membrane-bound spores are removed and the medium is stained. The extent of germination is assessed by microscopic examination of the spores and the presence of active hydrolytic enzymes is revealed by the staining. The staining methods are sensitive; detection limits are 1 X 10(-3) unit of cellulase; 2 X 10(-4) unit of protease; 3 X 10(-3) unit of pectin lyase; 3.5 units of polygalacturonase; 2 X 10(-3) unit of pectin methyl esterase. The method has been demonstrated by studying the production of enzymes by germinating conidia of Botrytis cinerea. Cellulase and protease were present before any spores germinated. Pectin lyase was first observed when at least 80% of the spores had germinated. Pectin methyl esterase and polygalacturonase were not produced by the spores.

Cellulase↗
PubMedDate not supplied

Effect of pectinase on rumen fermentation in sheep and lambs.

In trial with adult wethers and weaned lambs the effect of enzymatic preparation Pektofoetidin G3x (mostly pectinase and cellulase) on rumen fermentation was studied. After 4 weeks of Pektofoetidin G3x application (0.54 g per day and animal) to adult wethers no statistically significant differences in total volatile fatty acids (VFA), acetic acid, propionic acid, butyric acid, ammonia in the rumen contents and urea in blood were determined between control and enzyme treated group. In comparison of fermentation parameters in wethers (mean of 1-3 hours after feeding) and lambs (2-3 hours after feeding) the significant differences in mol % of acetic acid (63.3 in control, 54.6 in experimental group, P less than 0.01), propionic acid (24.6, vs. 31.3, P less than 0.001), acetate: proprionate ratio (2.54, vs. 1.77, P less than 0.01) and in energy efficiency of VFA production (76.0%, vs. 79.1%, P less than 0.001) were determined. These differences between wethers and lambs suggest more intensive fermentation in lambs than in adult sheep. On the basis of these results it is possible to suggest, that in adult animals the efficiency of application of enzymatic preparations is low. In utilization of enzymatic preparations more important role, probably, is that of ruminal ecosystem itself, that, if once fully developed, is perfectly resistant to biotechnological interferences.

Acetates↗
PubMed1985

Cloning and expression in Escherichia coli of pectinase genes of Erwinia carotovora subsp. carotovora.

Genes coding for an endo-pectate lyase, an exo-pectate lyase, and an endopolygalacturonase of Erwinia carotovora subsp. carotovora Ecc71 were cloned in Escherichia coli HB101, using the cosmid pHC79. The products of the cloned pectinase genes paralleled their counterparts in strain Ecc71 in isoelectric mobility, mode of substrate degradation, and ability to macerate potato tuber tissue.

Cloning, Molecular↗
PubMed1977

[Studies of the chronic toxicity of mold pectinase].

Studied was the action of mould pectinase produced in this country, using Asp. niger. Rats and guinea pigs were subject to the testing through continuous oral treatment. The preparation was mixed with feed at 0.1 and 0.2 ratio percents (1000 and 2000 ppm)--with the rats for a period of 90 days, and with the guinea pigs--in the course of 180 days. It was found that the enzyme preparation stimulates the growth (more strongly expressed in rats), showing no adverse effect on the appetite and behaviour as well as on the tested clinical and biochemical indices of the blood and urine and the structure and development of viscera and the reproductive capacity of the test animals. The positive effect on the growth of animals is explained by the better utilization of the nutrient components of the ration, and the harmlessness of the preparation--by its weak resorption in the digestive tract (resorption index 13) and the fact that it is not able to attack animal tissues having no pectin substances.

Administration, Oral↗
PubMed1991

Inducing properties of analogs of 2-keto-3-deoxygluconate on the expression of pectinase genes of Erwinia chrysanthemi.

In Erwinia chrysanthemi, all the genes involved in pectin degradation are controlled by the negative regulatory gene kdgR. 2-keto-3-deoxy-gluconate (KDG) is the inducing molecule that interacts with KdgR to allow the expression of all the genes of the kdg regulon. The inducing properties on the expression of genes regulated by kdgR of various analogs and derivatives of KDG were tested. All the inducers share the common moiety COOH-CO-CH2-CHOH-C-C included in a pyranic cycle. Our results show that esterification of C1 prevents induction. Presence of a ketone function on C2 and absence of hydroxyl on C3 are necessary for induction. The nature and the configuration of substituent on C5 has no influence on induction. Two compounds have interesting properties: 5-O-methyl-KDG is a gratuitous inducer, and gluconic acid can prevent induction.

Erwinia↗
PubMed1979

Activity of pectinases, amylases, and saccharase in Pythium spp.

The activity of pectine-lyase, polygalacturonase, pectine-methyl-esterase, amylase, and saccharase in Pythium ultimum, Pythium oligandrum, and Pythium debaryanum was determined. Cultures of fungi were cultivated under different temperatures and pH-values within 24 hours and 15 days. The optimum temperature for production of the mentioned enzymes was found to be 24 degrees C. Furthermore, the influence of pH and age of culture on activity of enzyme was investigated. The same trend was found in all the fungus species examined.

Amylases↗