Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides

Vries, Ronald P. de; Kester, H.C.M.; Poulsen, Charlotte; Benen, J.A.E.; Visser, Jaap

doi:10.1016/s0008-6215(00)00066-5

Cited by 243 publications

(139 citation statements)

References 44 publications

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“…Synergism between different xylanases, between xylanases and the associated binding modules, and between xylanases and esterases has also been reported (e.g. Suh et al, 1996b;Fernandes et al, 1999;de Vries et al, 2000).…”

Section: Introductionmentioning

confidence: 84%

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

et al. 2004

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Four extracellular enzymes of the thermophilic bacterium Clostridium stercorarium are involved in the depolymerization of de-esterified arabinoxylan: Xyn11A, Xyn10C, Bxl3B, and Arf51B. They were identified in a collection of eight clones producing enzymes hydrolysing xylan (xynA, xynB, xynC), b-xyloside (bxlA, bxlB, bglZ) and a-arabinofuranoside (arfA, arfB). The modular enzymes Xyn11A and Xyn10C represent the major xylanases in the culture supernatant of C. stercorarium. Both hydrolyse arabinoxylan in an endo-type mode, but differ in the pattern of the oligosaccharides produced. Of the glycosidases, Bxl3B degrades xylobiose and xylooligosaccharides to xylose, and Arf51B is able to release arabinose residues from de-esterified arabinoxylan and from the oligosaccharides generated. The other glycosidases either did not attack or only marginally attacked these oligosaccharides. Significantly more xylanase and xylosidase activity was produced during growth on xylose and xylan. This is believed to be the first time that, in a single thermophilic micro-organism, the complete set of enzymes (as well as the respective genes) to completely hydrolyse de-esterified arabinoxylan to its monomeric sugar constituents, xylose and arabinose, has been identified and the enzymes produced in vivo. The active enzyme system was reconstituted in vitro from recombinant enzymes.

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Section: Introductionmentioning

confidence: 84%

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

et al. 2004

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“…These enzymes are severely hindered in their activity by the presence of acetyl residues on the main chain and require the presence of rhamnogalacturonan acetyl esterase (see "Acetyl-and methylesterases" below) for efficient hydrolysis of the rhamnogalacturonan backbone (90). Also characterized are two exo-acting enzymes, rham- nogalacturonan rhamnohydrolase (265) and rhamnogalacturonan galacturonohydrolase (264), that further degrade the oligosaccharides from the nonreducing end.…”

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

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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“…Both RG-lyase and RG-hydrolase display an increase in catalytic efficiency towards deacetylated RG-I, thus these enzymes work synergistically with RGAE to degrade RG-I [13]. The mature RG-lyase has 508 residues with a calculated molecular weight of 54202.9 Da, pI 5.2 and optimal activity at pH 6.0 and 50°C [10].…”

Section: Introductionmentioning

confidence: 99%

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

MCDONOUGH¹

2004

FEBS Letters

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Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves a-1,4 glycosidic bonds between L L -rhamnose and D D -galacturonic acids in the backbone of rhamno galacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RGlyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes.

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Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides

Cited by 243 publications

References 44 publications

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

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