Characterization of a novel endopolygalacturonase from<i>Aspergillus niger</i>with unique kinetic properties

Pařenicová, Lucie; Kester, H.C.M.; Benen, J.A.E.; Visser, Jaap

doi:10.1016/s0014-5793(00)01173-x

Cited by 56 publications

(41 citation statements)

References 17 publications

(44 reference statements)

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“…Six types of hydrolases have been identified in aspergilli. Several endopolygalacturonases are produced that all cleave within the pectin smooth region (10,185,284), whereas exopolygalacturonases cleave at the nonreducing terminal end of this region (35,139,182,259). The A. aculeatus and A. tubingensis exopolygalacturonases were able to release galacturonic acid from polygalacturonic acid, sugar beet pectin, and xylogalacturonan (35,180,182).…”

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

“…It also released the dimer ␤-Xyl-(1,3)-GalA from xylogalacturonan, indicating that the action of the enzyme is not hindered by the presence of xylose on the terminal galacturonic acid residue. The seven endopolygalacturonases produced by A. niger differ in their specific activity (varying from 25 to 4,000 U/mg), sensitivity to methylation of the substrate (36,183,281,284), and mode of action. Four of the enzymes (endopolygalacturonases I, A, C, and D) show processive behavior, also known as multiple attack on a single chain (36,281,284), whereas the other three enzymes (endopolygalacturonases II, B, and E) work via a single-attack mechanism (36,281,284).…”

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

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AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

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878

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

Self Cite

878

585

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“…The best-characterized (fungal) endo-PG enzyme requires four to five consecutive runs of unesterified GalUA residues for cleavage Pařenicová et al, 2000). However, little is known about the enzyme activity and substrate specificity of most plant PGs.…”

Section: Introductionmentioning

confidence: 99%

ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1), ADPG2, and QUARTET2 Are Polygalacturonases Required for Cell Separation during Reproductive Development inArabidopsis

et al. 2009

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Cell separation is thought to involve degradation of pectin by several hydrolytic enzymes, particularly polygalacturonase (PG). Here, we characterize an activation tagging line with reduced growth and male sterility caused by increased expression of a PG encoded by QUARTET2 (QRT2). QRT2 is essential for pollen grain separation and is part of a small family of three closely related endo-PGs in the Arabidopsis thaliana proteome, including ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1) and ADPG2. Functional assays and complementation experiments confirm that ADPG1, ADPG2, and QRT2 are PGs. Genetic analysis demonstrates that ADPG1 and ADPG2 are essential for silique dehiscence. In addition, ADPG2 and QRT2 contribute to floral organ abscission, while all three genes contribute to anther dehiscence. Expression analysis is consistent with the observed mutant phenotypes. INDEHISCENT (IND) encodes a putative basic helix-loop-helix required for silique dehiscence, and we demonstrate that the closely related HECATE3 (HEC3) gene is required for normal seed abscission and show that IND and HEC3 are required for normal expression of ADPG1 in the silique dehiscence zone and seed abscission zone, respectively. We also show that jasmonic acid and ethylene act together with abscisic acid to regulate floral organ abscission, in part by promoting QRT2 expression. These results demonstrate that multiple cell separation events, including both abscission and dehiscence, require closely related PG genes.

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“…4) indicating an exo-manner of substrates cleavage. Only one case of PG, but of microbial origin, with the ability to cleave dimer is known (Parenicová et al 2000).…”

Section: Resultsmentioning

confidence: 99%

Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots

et al. 2009

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Abstract:The main form of pectate hydrolases in the cell wall of parsley roots showed a unique substrate preference of a plant exopolygalacturonase because it clearly preferred the substrates with degree of polymerization about 10. This form was separated from the others, purified and characterized. Enzyme exhibited sharp pH optimum corresponding to pH 4.7, molecular mass 53.5 kDa, and isoelectric point 5.3. It was stable at 50• C in 2-h assay and had optimum of temperature at 60• C (activation energy being 37.0 kJ/mol). The interaction with concanavalin A indicated the glycosylation of enzyme. Substrates were cleaved from the non-reducing end.

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Characterization of a novel endopolygalacturonase fromAspergillus nigerwith unique kinetic properties

Cited by 56 publications

References 17 publications

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1), ADPG2, and QUARTET2 Are Polygalacturonases Required for Cell Separation during Reproductive Development inArabidopsis

Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots

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