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PubMed2004

Pectinase production by Aspergillus niger using wastewater in solid state fermentation for eliciting plant disease resistance.

An elicitor of plant disease resistance, pectinase, was produced by solid state fermentation with Aspergillus niger. Sugar beet pulp was used as carbon source and the wastewater from monosodium glutamate production was used as nitrogen and water source. The composition of the fermentation medium was: 11 ml concentrated wastewater (containing NH3-N 38.2 mg/ml), sugar beet pulp 10 g, Na2HPO4.12H2O 0.2 g, KH2PO4 0.04 g in a 500 ml Erlenmeyer flask. The fermentation temperature was 30 degrees C and the relative humidity of the air was 75-90%. The maximum production of pectinase was reached after 96 h cultivation. The crude pectinase extracted from the fermented materials could elicit disease resistance in cucumber and tomato seedlings.

Aspergillus niger↗
PubMed2006

Hydrolysis of grapefruit peel waste with cellulase and pectinase enzymes.

Approximately 1 million metric tons of grapefruit were processed in the 2003/04 season resulting in 500,000 metric tons of peel waste. Grapefruit peel waste is usually dried, pelletized, and sold as a low-value cattle feed. This study tested different loadings of commercial cellulase and pectinase enzymes and pH levels to hydrolyze grapefruit peel waste to produce sugars. Pectinase and cellulase loadings of 0, 1, 2, 5, and 10mgprotein/g peel dry matter were tested at 45 degrees C. Hydrolyses were supplemented with 2.1mg beta-glucosidase protein/g peel dry matter. Five mg pectinase/g peel dry matter and 2mgcellulase/g peel dry matter were the lowest loadings to yield the most glucose. Optimum pH was 4.8. Cellulose, pectin, and hemicellulose in grapefruit peel waste can be hydrolyzed by pectinase and cellulase enzymes to monomer sugars, which can then be used by microorganisms to produce ethanol and other fermentation products.

Carbohydrates↗
PubMed2006

Preparation and properties of immobilized pectinase onto the amphiphilic PS-b-PAA diblock copolymers.

Well-defined amphiphilic block copolymers poly(styrene-b-acrylic acid) (PS-b-PAA) with controlled block length were synthesized using atom transfer radical polymerization (ATRP). Pectinase enzyme was immobilized on the well-defined amphiphilic block copolymers PS-b-PAA. The carboxyl groups on the amphiphilic PS-b-PAA diblock copolymers present a very simple, mild, and time-saving process for enzyme immobilization. Various characteristics of immobilized pectinase such as the pH and temperature stability, thermal stability, and storage stability were valuated. Among them the pH optimum and temperature optimum of free and immobilized pectinase were found to be pH 6.0 and 65 degrees C.

Acrylates↗
PubMed2000

Pectinase in papermaking: solving retention problems in mechanical pulps bleached with hydrogen peroxide.

Treatment with the enzyme pectinase has been reported to lower the cationic demand of thermomechanical pulp (TMP) bleached with alkaline peroxide in the laboratory. We have extended this discovery to bleached TMP produced industrially, and shown that commercial enzyme preparations can treat pulp within 15 min at the temperature and pH values prevalent in paper mills. About half of the cationic demand in the bleached pulp can be destroyed by pectinase. Dynamic drainage jar experiments show that the enzyme treatment improves the effectiveness of several cationic polymers to increase retention of fines and filler particles. It does not increase retention in the absence of retention aids or with nonionic polymers, and does not damage the strength properties of the pulp. Pectinase could be easily incorporated into paper machine stock preparation systems to lower the charges of cationic retention aids needed in furnishes containing peroxide-bleached mechanical pulp.

Journal Article↗
PubMedDate not supplied

Affinity precipitation and macroaffinity ligand facilitated three-phase partitioning for refolding and simultaneous purification of urea-denatured pectinase.

Protein refolding is an integral step in the recovery of protein activity from inclusion bodies. It is shown that affinity precipitation and macroaffinity ligand facilitated three-phase partitioning (MLFTPP) led to refolding of urea-denatured pectinase present in a commercial preparation, with simultaneous purification. Affinity precipitation consists of precipitation of the desired enzyme by complexing it with a suitable stimulus-sensitive macroaffinity ligand. This ligand in this case was alginate/esterified alginate. The complex of the polymer-pectinase could be precipitated by adding calcium ions. In MLFTPP (carried out by adding tertiary butanol and ammonium sulfate to the aqueous solution of crude enzyme and the polymer), the polymer or its complex with the enzyme form an interfacial precipitate between tert-butyl alcohol phase and aqueous phase. It is believed that in both processes, while molecular recognition of alginate/esterified alginate to pectinase facilitates their selective binding to the enzyme, the correct refolding is facilitated by preventing molecular aggregation of unfolded enzyme molecules. Three-phase partitioning with esterified alginate as the macroaffinity ligand gave 100% recovery with 4-fold purification. Affinity precipitation with 1% alginate gave 52% yield with 18-fold purification. On the other hand, use of 0.5% esterified alginate gave only 7-fold purification but with 75% recovery of activity.

Affinity Labels↗
PubMed1993

Conidial and mycelial-bound exo-pectinase of Aspergillus sp.

Intact conidia of Aspergillus sp. were able to degrade pectin 'in vitro' even when protein synthesis was inhibited, thus indicating the presence of cell bound pectinases. At least an exo-pectinase was found and this enzyme was also present in the mycelium of Aspergillus sp. Its presence was not dependent on the carbon source used for growth, suggesting its constitutive nature. This exo-pectinase could be released from conidia or mycelium by incubation at different pH values and the amount of enzyme released could be increased by treatments with chemical agents and hydrolytic enzymes.

Aspergillus↗
PubMed2002

Improvement of tea leaves fermentation with Aspergillus spp. pectinase.

The pectinase enzymes isolated from Aspergillus spp., A. indicus, A. flavus and A. niveus were used for fermentation of tea leaves. The enzymes were purified and characterized. The effect of both crude enzyme preparation and purified pectinase enzymes on the improvement of tea leaf fermentation were determined in terms of theaflavin, thearubigin, high polymerized substances, total liquor colour, dry matter content and total soluble solids of the tea produced. The crude enzyme preparations obtained from ethanol precipitation were found to be more effective in improving tea leaf fermentation than the purified pectinase enzymes.

Journal Article↗
PubMedDate not supplied

[Biosynthesis of pectinase by fungi Bjerkandera and Coriolus by solid phase fermentation].

Production of an extracellular pectinase by wood-rot fungi of the genus Bjerkandera and Coriolus was studied. The active producers B. adusta 40 and C. versicolor 24 were selected. The dynamics of production of pectinase and effects of temperature, initial pH, humidity of the medium and addition of nitrogen sources on the biosynthesis of pectinase were studied.

Fermentation↗
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↗
PubMed2000

Sequential synthesis and secretion of pectinases by Penicillium frequentans.

Penicillium frequentans synthesized eleven polygalacturonases and three pectinesterases when grown in the presence of pectin, sodium polypectate or monogalacturonic acid. When glucose was the sole carbohydrate source in the medium two of these polygalacturonases and one pectinesterase were produced. The enzymes produced under any of these conditions degraded pectic substrates to monogalacturonic acid, suggesting that this monosaccharide or its metabolites should induce the pectinolytic complex. All pectinesterases and most of the extracellular polygalacturonases were synthesized after the 2nd hour of incubation. The pectinases produced by Penicillium frequentans were not secreted at the same time but after 5 hours of incubation all of them could be detected outside the cell those detected only inside the cell were probably membrane-associated or unglycosylated forms of the extracellular pectinases.

Carbon↗
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↗
PubMed1993

New approach for selecting pectinase producing mutants of Aspergillus niger well adapted to solid state fermentation.

The aim of this paper is to review and study a new approach for improving strains of Aspergillus niger specially adapted to produce pectinases by Solid State Fermentation (SSF) with materials having low levels of water activity (a(w)), i.e., coffee pulp. Special emphasis is placed on the use of two antimetabolic compounds: 2-deoxy-glucose (DG) and 2,4-dinitro-phenol (DNP) combined with a water depressant (ethylene glycol = EG) in order to put strong selection pressures on UV treated spores from parental strain C28B25 isolated from a coffee plantation. Such a strain was found to be DG sensitive. Results suggested the existence of a reciprocal relation between adaptation of isolated strains to SSF or to Submerged Fermentation (SmF) systems. Preliminary physiological analysis of isolated strains showed that at least some few initially DG resistant mutants could revert to DG sensitive phenotype but conserving increased pectinase production. Also it was found that phenotype for DNP resistance could be associated to changes of DG resistance. Finally, it was found that low levels of a(w) produced by adding 15% EG to agar plates, were a significant selection factor for strains well adapted to SSF system.

Journal Article↗
PubMed2005

A marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods.

The production of a highly alkaline and thermostable pectinase of Bacillus pumilus was optimized in submerged fermentation using Plackett-Burman design and response surface methodology. Three fermentation variables (C:N ratio, K(2)HPO(4), and pH), which were identified to significantly affect pectinase production by Plackett-Burman design were further optimized using response surface methodology of central composite design (CCD). An over all 34- and 41-fold increase in enzyme production was achieved in shake flasks and lab fermenter by the optimization of variables using statistical approaches, respectively. The enzyme was optimally active at pH 10.5 and 50 degrees C, and selectively degraded only the noncellulosic gummy material of ramie (Boehmeria nivea) fibres causing 10.96% fibre weight loss, and therefore, the enzyme could find application in fibre processing industry. The use of the enzyme in fibre processing reduces the use of alkali, and the associated alkalinization of water bodies.

Bacillus↗
PubMed2002

SCP and crude pectinase production by slurry-state fermentation of lemon pulps.

Single cell protein (SCP) and crude pectinolytic enzymes production from citrus pulps is reported. SCP and enzymes were produced by slurry-state flask cultivation of Aspergillus niger and Trichoderma viride on pulps from lemon juice clarification. Production as well as crude pectinase activity was not affected by the high dry matter content of the pulps. Both the protein content in the residue and the enzyme activity in the supernatant were higher in T. viride than in A. niger culture. The crude pectinase of T. viride, whose specific activity was similar to that found for a commercial concentrated preparation, could be utilized in the same citrus processing factory as well as in other factories which use large amounts of pectinolytic crude preparations, for example to enhance depuration plant performance.

Aspergillus niger↗
PubMed1999

Performance of selected microbial pectinases on synthetic monomethyl-esterified di- and trigalacturonates.

Two monomethyl esters of alpha-(1-4)-linked D-galacturonic dimers and three monomethyl esters of alpha-(1-4)-linked D-galacturonic acid trimers were synthesized chemically and further used as substrates in order to establish the substrate specificity of six different endopolygalacturonases from Aspergillus niger, one exopolygalacturonase from Aspergillus tubingensis, and four selected Erwinia chrysanthemi pectinases; exopolygalacturonan hydrolase X (PehX), exopolygalacturonate lyase X (PelX), exopectate lyase W (PelW), and oligogalacturonan lyase (Ogl). All A. niger endopolygalacturonases (PGs) were unable to hydrolyze the two monomethyldigalacturonates and 2-methyltrigalacturonate, whereas 1-methyltrigalacturonate was only cleaved by PGI, PGII, and PGB albeit at an extremely low rate. The hydrolysis of 3-methyltrigalacturonate into 2-methyldigalacturonate and galacturonate by all endopolygalacturonases demonstrates that these enzymes can accommodate a methylgalacturonate at subsite -2. The A. tubingensis exopolygalacturonase hydrolyzed the monomethyl-esterified digalacturonates and trigalacturonates although at lower rates than for the corresponding oligogalacturonates. 1-Methyltrigalacturonate was hydrolyzed at the same rate as trigalacturonate which demonstrates that the presence of a methyl ester at the third galacturonic acid from the nonreducing end does not have any effect on the performance of exopolygalacturonase. Of the four E. chrysanthemi pectinases, Ogl was the only enzyme able to cleave digalacturonate, whereas all four enzymes cleaved trigalacturonate. Ogl does not cleave monomethyl-esterified digalacturonate and trigalacturonate in case the second galacturonic acid residue from the reducing end is methyl-esterified. PehX did not hydrolyze any of the monomethyl-esterified trigalacturonates. The two lyases, PelX and PelW, were both only able to cleave 1-methyltrigalacturonate into Delta4,5-unsaturated 1-methyldigalacturonate and galacturonate.

Aspergillus↗
PubMed2005

A mixture of pure cellulase, hemicellulase and pectinase improves broiler performance.

1. The effects of a mixture of pure enzymes (cellulase, hemicellulase and pectinase) and a commercial enzyme, Energex, were examined on performance and metabolisabilities in broiler chicks given a maize-soybean meal diet. Composition of the mixed enzyme was similar to Energex except that protease was not present. 2. Chicks were divided into three groups: control, mixed enzyme and Energex with 7 replicates per group. Male broiler chicks were raised at 25 degrees C in wire-floored cages for 12 d from 15 d of age. Feed and water were offered ad libitum. 3. The Energex group gained significantly more weight and the mixed enzyme group tended to gain more than the control. Feed intakes were similar and thus the feed conversion ratio of Energex was significantly improved while it tended to be improved by the mixed enzyme. 4. The mixed enzyme group showed significant improvement in carcase and muscle weight when compared with the control group. The mixed enzyme group also showed significant improvement in organic matter and crude protein metabolisabilities. In the groups given enzyme, abdominal fat weight tended to decrease. 5. It is concluded that a combination of cellulase, hemicellulase and pectinase is effective in improving organic matter and crude protein metabolisabilities and carcase yield of broilers on a maize-soybean meal diet.

Animal Feed↗
PubMed2003

Comparative study of regulatory mechanisms for pectinase production by Erwinia carotovora subsp. carotovora and Erwinia chrysanthemi.

The production of pectinase, the major virulence determinant of soft-rot Erwinia species, is controlled by many regulatory factors. We focused on the major regulatory proteins, KdgR, CRP, Pir, and PecS, characterized mainly in E. chrysanthemi, and tested for their presence and function in the control of pectate lyase (Pel) and polygalacturonase (Peh) production in E. carotovora subsp. carotovora. Homologues of kdgR and crp but not of pir and pecS were detected by Southern blot analyses in E. carotovora subsp. carotovora. In fact, KdgR and CRP homologues of E. carotovora subsp. carotovora had high amino acid identities to those of E. chrysanthemi, including a complete match of the hypothetical helix-turn-helix DNA-binding motif. However, in Western blot analyses using anti-Pir (E. chrysanthemi) antibodies, a cross-reacting protein was present in both Erwinia species, although Pel production in E. carotovora subsp. carotovora was not further stimulated by adding plant extract into the medium containing PGA (polygalacturonic acid) in which hyperinduction by Pir has been reported in E. chrysanthemi EC16. When plasmids that contained each of these regulatory genes from E. chrysanthemi were introduced into E. carotovora subsp. carotovora, Pel production was controlled as predicted from their roles in E. chrysanthemi, except for PecS. PecS exerted a positive control in E. carotovora subsp. carotovora, in contrast to a negative control in E. chrysanthemi. DNA-binding assays demonstrated that KdgR, CRP, Pir, and PecS of E. chrysanthemi and KdgR and CRP homologues of E. carotovora subsp. carotovora could bind to the promoter regions of pel-1, pel-3, and peh of E. carotovora subsp. carotovora. Taken together, KdgR and CRP homologues of E. carotovora subsp. carotovora may regulate Pel and Peh production as in E. chrysanthemi. However, the presence of Pir and PecS homologues in E. carotovora subsp. carotovora was not identified in this study, though these proteins of E. chrysanthemi were functional on the promoter regions of the pectinase genes of E. carotovora subsp. carotovora.

Amino Acid Sequence↗