Lignin-hemicellulose complexes restrict enzymatic solubilization of mannan and xylan from dissolving pulp

Gübitz, Georg; Stebbing, Derrick W.; Johansson, C. Ingemar; Saddler, John N.

doi:10.1007/s002530051310

Cited by 32 publications

(12 citation statements)

References 9 publications

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“…Endo-1,4-b-xylanase primarily randomly hydrolyzes xylan to xylooligomers, while b-xylosidase enzymes release monomeric xylose from the non-reducing ends of xylooligomers (Chen et al, 1997). The ability of these four enzymes in hydrolyzing xylooligomers to xylose not only depends on their endo-1,4-bxylanase and b-xylosidase activities but also on synergistic action of these two enzymes with esterases to remove acetyl substituents from the b-1,4-linked D xylose backbone of xylan (Coughlan and Hazlewood, 1993;Gubitz et al, 1998). In this study, xylooligomers with a DP range from 2 to 30 were grouped together as low DP xylooligomers, and those with a DP range over 30 were termed as high DP xylooligomers.…”

Section: Resultsmentioning

confidence: 97%

Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase

Qing

Wyman

2011

Bioresource Technology

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Section: Resultsmentioning

confidence: 97%

Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase

Qing

Wyman

2011

Bioresource Technology

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“…In xylan, ferulic acids are linked to arabinose and are then attached to a xylan backbone, while in pectin, ferulic acids are ester linked to pectin polysaccharides mainly through arabinose or galactose (37). These cross-links formed via ferulic acids dramatically reduce the biodegradability of plant cell walls by microorganisms (7,23).…”

mentioning

confidence: 99%

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Cai

Luo

et al. 2011

Appl Environ Microbiol

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Feruloyl esterases (Faes) constitute a subclass of carboxyl esterases that specifically hydrolyze the ester linkages between ferulate and polysaccharides in plant cell walls. Until now, the described microbial Faes were mainly from fungi. In this study, we report that Cellulosilyticum ruminicola H1, a previously described fibrolytic rumen bacterium, possesses three different active feruloyl esterases, FaeI, FaeII, and FaeIII. Phylogenetic analysis classified the described bacterial Faes into two types, FaeI and FaeII in type I and FaeIII in type II. Substrate specificity assays indicated that FaeI is more active against the ester bonds in natural hemicelluloses and FaeIII preferentially attacks the ferulate esters with a small moiety, such as methyl groups, while FaeII is active on both types of substrates. Among the three feruloyl esterase genes, faeI was the only one induced significantly by xylose and xylan, while pectin appeared to moderately induce the three genes during the late log phase to stationary phase. Western blot analysis determined that FaeI and FaeIII were secreted and cytoplasmic proteins, respectively, whereas FaeII seemed to be cell associated. The addition of FaeI and FaeII but not FaeIII enhanced the activity of a xylanase on maize cob, suggesting a synergy of the former two with xylanase. Hence, we propose that the three feruloyl esterases work in concert to hydrolyze ferulate esters in natural hemicelluloses.

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“…Ferulic acids can also be found forming several types of dehydrodimers (17,20,21,26) and can be involved in ester and/or ether linkages with lignin components (4,26). Hydroxycinnamates can therefore be seen as important structural components, providing cell wall integrity and hence protecting plants against digestion by plant-invading microorganisms (8,18,22).…”

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confidence: 99%

Purification and Properties of a Feruloyl Esterase Involved in Lignocellulose Degradation byAureobasidium pullulans

Rumbold

Biely

Mastihubová

et al. 2003

Appl Environ Microbiol

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The lignocellulolytic fungus Aureobasidium pullulans NRRL Y 2311-1 produces feruloyl esterase activity when grown on birchwood xylan. Feruloyl esterase was purified from culture supernatant by ultrafiltration and anion-exchange, hydrophobic interaction, and gel filtration chromatography. The pure enzyme is a monomer with an estimated molecular mass of 210 kDa in both native and denatured forms and has an apparent degree of glycosylation of 48%. The enzyme has a pI of 6.5, and maximum activity is observed at pH 6.7 and 60°C.

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Lignin-hemicellulose complexes restrict enzymatic solubilization of mannan and xylan from dissolving pulp

Cited by 32 publications

References 9 publications

Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase

Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Purification and Properties of a Feruloyl Esterase Involved in Lignocellulose Degradation byAureobasidium pullulans

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