Application of xylanases in the pulp and paper industry

Büchert, Johanna; Tenkanen, Maija; Kantelinen, Anne; Viikari, Liisa

doi:10.1016/0960-8524(94)90222-4

Cited by 83 publications

(37 citation statements)

References 28 publications

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“…␤-1,4-Glycanases are of considerable utility in the pulp and paper industry (51), as additives for the baking industry, and in biomass conversion (52). More important, the MS-ABPP approach is also applicable to a wide range of retaining endoglycosidases.…”

Section: Discussionmentioning

confidence: 99%

Active-site Peptide “Fingerprinting” of Glycosidases in Complex Mixtures by Mass Spectrometry

Hekmat¹,

Kim²,

Williams³

et al. 2005

Journal of Biological Chemistry

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New proteomics methods are required for targeting and identification of subsets of a proteome in an activity-based fashion. Here, we report the first gel-free, mass spectrometry-based strategy for mechanism-based profiling of retaining ␤-endoglycosidases in complex proteomes. Using a biotinylated, cleavable 2-deoxy-2-fluoroxylobioside inactivator, we have isolated and identified the active-site peptides of target retaining ␤-1,4-glycanases in systems of increasing complexity: pure enzymes, artificial proteomes, and the secreted proteome of the aerobic mesophilic soil bacterium Cellulomonas fimi. The active-site peptide of a new C. fimi ␤-1,4-glycanase was identified in this manner, and the peptide sequence, which includes the catalytic nucleophile, is highly conserved among glycosidase family 10 members. The glycanase gene (GenBank TM accession number DQ146941) was cloned using inverse PCR techniques, and the protein was found to comprise a catalytic domain that shares ϳ70% sequence identity with those of xylanases from Streptomyces sp. and a family 2b carbohydrate-binding module. The new glycanase hydrolyzes natural and artificial xylo-configured substrates more efficiently than their cello-configured counterparts. It has a pH dependence very similar to that of known C. fimi retaining glycanases.With the completion of the genome sequences of many organisms, the field of proteomics faces several major tasks. One challenge is that of identification and assignment of structure/function to the tens of thousands of proteins encoded by prokaryotic and eukaryotic genomes. Another challenge is accurate quantitative analysis of changes in protein levels/activities that occur within a proteome as a response to biological perturbations that are due either to normal developmental and metabolic changes or to abnormalities associated with disease. Proteomic techniques such as comparative two-dimensional gel electrophoresis coupled with mass spectrometry, the isotope-coded affinity tagging approach (1), and variations of isotope-coded affinity tagging that identify sites of modification (e.g. glycosylation and phosphorylation) on proteins (2-4) fail to provide a direct assessment of protein function.Recently, several chemical strategies for activity-based protein profiling (ABPP) 4 in complex proteomes that target several enzyme groups, including oxidoreductases (5, 6), serine hydrolases (7, 8), cysteine proteases (9, 10), threonine proteases (11), metalloproteases (12), protein phosphatases (13), kinases (14), and exoglycosidases (15), have been employed. ABPP probes have two general features: 1) an active sitedirected (mechanism-based) inactivator or affinity label that reacts with a catalytic residue and forms a covalent adduct with the target enzyme(s) and 2) one or more reporter groups that enable rapid detection (e.g. a fluorophore) and/or affinity isolation (e.g. biotin) (16). As such, ABPP methods can provide direct information on post-translational forms of protein regulation (17). However, most of the ABPP research ...

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Section: Discussionmentioning

confidence: 99%

Active-site Peptide “Fingerprinting” of Glycosidases in Complex Mixtures by Mass Spectrometry

Hekmat¹,

Kim²,

Williams³

et al. 2005

Journal of Biological Chemistry

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“…4 The members of both families have been extensively studied and certain enzymes, most frequently from GH11, have been incorporated into industrial processes. [5][6][7] The GH10 family members all possess a catalytic domain, which exhibits (b/a) 8 architecture and displays an average molecular mass of approximately 40 kDa. The GH11 members are generally smaller (approximately 20 kDa) and display a b-jelly roll structure.…”

Section: Introductionmentioning

confidence: 99%

Impact and efficiency of GH10 and GH11 thermostable endoxylanases on wheat bran and alkali-extractable arabinoxylans

Beaugrand

Chambat

Wong

et al. 2004

Carbohydrate Research

132

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“…Hand sheets were prepared from the treated pulp and the quality parameters were determined. For chlorine treatment, a portion of the enzyme-pretreated pulp was subjected to the conventional chlorine extraction sequence proposed by Buchert et al (1992). Hand sheets were prepared from the treated pulp and the quality parameters were determined.…”

Section: Methodsmentioning

confidence: 99%

Application of Aspergillus fumigatus Xylanase for Quality Improvement of Waste Paper Pulp

Savitha

Sadhasivam

Swaminathan

2007

Bull Environ Contam Toxicol

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Application of xylanases in the pulp and paper industry

Cited by 83 publications

References 28 publications

Active-site Peptide “Fingerprinting” of Glycosidases in Complex Mixtures by Mass Spectrometry

Active-site Peptide “Fingerprinting” of Glycosidases in Complex Mixtures by Mass Spectrometry

Impact and efficiency of GH10 and GH11 thermostable endoxylanases on wheat bran and alkali-extractable arabinoxylans

Application of Aspergillus fumigatus Xylanase for Quality Improvement of Waste Paper Pulp

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