Isolation and characterization of an endopolygalacturonase from Phanerochaete chrysosporium

Shanley, Nancy; Broek, L.A.M. van den; Voragen, A.G.J.; Coughlan, Michael P.

doi:10.1016/0168-1656(93)90169-n

Cited by 24 publications

(11 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…ciceri reduced the viscosity by 14 and 8%, respectively, after 4% hydrolysis of substrate suggesting that these two enzymes are exoenzymes. In contrast, to be classified as an endoenzyme, the rate of decrease in viscosity must exceed the rate of release of reducing sugars [45,46]. For PG isolated from M. flavus [29], the specific viscosity of PGA and esterified pectin (DE 89%) were decreased by 50 and 40%, respectively, in 10 min at 30°C but released only small amounts of reducing sugars suggesting that the enzyme acts in an endo-manner.…”

Section: Discussionmentioning

confidence: 91%

Characterization of an Exopolygalacturonase from Aspergillus niger

Fahmy

El-Beih

Mohamed

et al. 2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Polygalacturonase (PGI) from Aspergillus niger NRRL3 was purified about 12.0-fold from the cell-free broth using diethylaminoethyl-Sepharose and Sephacryl S-200 columns. The molecular weight of the PGI was 32,000 Da as estimated by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. PGI had an isoelectric point of 7.6 and an optimum pH of 5.0. PGI was active on polygalacturonic acid and esterified pectins, but the activity on pectin decreased with an increase in degree of esterification. PGI had higher affinity (low Km) and turnover number (Vmax/Km and Kcat/Km) toward polygalacturonic acid. PGI was found to have a temperature optimum at 40 degrees C and was approximately stable up to 30 degrees C. All the examined metal cations had partial inhibitory effects on PGI, while Mn+2 at 5 mM caused a complete inhibition for the enzyme. Comparison of viscosity reduction rates with release of reducing sugars indicated that the enzyme from A. niger is exoacting. The storage stability study of PGI showed that the enzyme in powder form retained 56% of its activity after 9 months of storage at 4 degrees C. The above properties of PGI may be suitable for food processing.

show abstract

Section: Discussionmentioning

confidence: 91%

Characterization of an Exopolygalacturonase from Aspergillus niger

Fahmy

El-Beih

Mohamed

et al. 2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…Enzymatic degradation of pit membranes has also been observed in whiterot fungi (Tsuneda et al 1987). Shanley et al (1993) characterized endopolygalacturonase (endo-PG) from the white-rot fungus Phanerochaete chrysosporium. Degradation of pit membranes by microbial enzymes is well documented .…”

Section: Introductionmentioning

confidence: 99%

Production of Polygalacturonase and Increase of Longitudinal Gas Permeability in Southern Pine by Brown-Rot and White-Rot Fungi

Green¹,

Clausen²

1999

Holzforschung

View full text Add to dashboard Cite

Hydrolysis of bordered and pinoid pits may be a key event during colonization of wood by decay fungi. Although pits are numerous, studies of pectin-hydrolyzing enzymes in wood decay fungi are scarce, probably because of the relatively low content (less than 4 %) of pectin in wood and because of the primary focus on understanding the degradation of lignified components. Endopolygalacturonase (endo-PG) activity was estimated by cup-plate assay and viscosity reduction of pectin from liquid cultures of fifteen brown-rot and eight white-rot basidiomycetous fungi using sodium polypectate as the carbon source. Oxalic acid was estimated in liquid culture and related to mycelial weight of each fungus. Changes in longitudinal gas permeability of southern pine cores exposed to selected decay fungi in liquid culture were measured to determine the extent of hydrolysis of bordered pits. Twelve of fifteen brown-rot and six of eight white-rot fungi tested were positive for at least one of the polygalacturonase test methods. Accumulation of oxalic acid was detected in thirteen of fifteen brown-rot isolates and none of the white-rot fungi tested. Gas permeability of pine cores increased approximately fourfold among brown-rot fungi tested and eighteenfold among white-rot fungi tested. Scanning electron microscopy revealed bordered pit membrane hydrolysis in cores colonized by white-rot fungi, but only torus damage, weakening and tearing of the pit membranes, was observed in cores exposed to brown-rot fungi. We conclude that both brown-and white-rot decay fungi have the enzymatic capacity to hydrolyze pectin, damage bordered pit membranes, and increase wood permeability during colonization and incipient decay. KeywordsWood decay Brown-rot White-rot Fungi Pit membrane Polygalacturonase Oxalic acid Brought to you by |

show abstract

“…Aspergilli produce variable hydrolases (endoand exopolygalacturonases, endorhamnogalacturonan hydrolases, rhamnogalacturonan rhamnohydrolase, ␣-rhamnosidase, and rhamnogalacturonan galacturonohydrolases) and lyases (pectin, pectate, and rhamnogalacturonan lyases), with several isoenzymes that differ in their specific activity (19). The pectinolytic enzymes of basidiomycetes isolated or characterized so far are endo/exorhamno-or polygalacturonases from the white rot fungus P. chrysosporium (147), the plant-pathogenic species Chondrostereum purpureum (148)(149)(150) and S. rolfsii (151,152), and the basidiomycete yeast Cystofilobasidium capitatum (153,154) as well as a rhamnogalacturonan lyase from the white rot fungus I. lacteus (155,156) (Table 11). However, there is a great potential to find novel pectinases from basidiomycetes with unique properties because of the diverse ecological niches that basidiomycetes inhabit and the variety of putative pectinase-encoding genes in their genomes (Table 4).…”

Section: Pectin-degrading Enzymesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

347

287

View full text Add to dashboard Cite

SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

show abstract

Isolation and characterization of an endopolygalacturonase from Phanerochaete chrysosporium

Cited by 24 publications

References 48 publications

Characterization of an Exopolygalacturonase from Aspergillus niger

Characterization of an Exopolygalacturonase from Aspergillus niger

Production of Polygalacturonase and Increase of Longitudinal Gas Permeability in Southern Pine by Brown-Rot and White-Rot Fungi

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Contact Info

Product

Resources

About