Occurrence and Biocatalytic Potential of Carbohydrate Oxidases

Hellemond, Erik W. van; Leferink, Nicole G. H.; Heuts, Dominic P. H. M.; Fraaije, Marco W.; Berkel, Willem J.H. van

doi:10.1016/s0065-2164(06)60002-6

Cited by 94 publications

(56 citation statements)

References 160 publications

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“…Glycolate oxidases are classified in CAZy as family AA7. In this family, we found gluco-oligosaccharide oxidases capable of oxidizing a variety of carbohydrates and possibly involved in the biotransformation of lignocellulosic compounds [64]. …”

Section: Discussionmentioning

confidence: 99%

Metataxonomic profiling and prediction of functional behaviour of wheat straw degrading microbial consortia

Jiménez

Dini‐Andreote

Elsas

2014

Biotechnol Biofuels

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BackgroundMixed microbial cultures, in which bacteria and fungi interact, have been proposed as an efficient way to deconstruct plant waste. The characterization of specific microbial consortia could be the starting point for novel biotechnological applications related to the efficient conversion of lignocellulose to cello-oligosaccharides, plastics and/or biofuels. Here, the diversity, composition and predicted functional profiles of novel bacterial-fungal consortia are reported, on the basis of replicated aerobic wheat straw enrichment cultures.ResultsIn order to set up biodegradative microcosms, microbial communities were retrieved from a forest soil and introduced into a mineral salt medium containing 1% of (un)treated wheat straw. Following each incubation step, sequential transfers were carried out using 1 to 1,000 dilutions. The microbial source next to three sequential batch cultures (transfers 1, 3 and 10) were analyzed by bacterial 16S rRNA gene and fungal ITS1 pyrosequencing. Faith’s phylogenetic diversity values became progressively smaller from the inoculum to the sequential batch cultures. Moreover, increases in the relative abundances of Enterobacteriales, Pseudomonadales, Flavobacteriales and Sphingobacteriales were noted along the enrichment process. Operational taxonomic units affiliated with Acinetobacter johnsonii, Pseudomonas putida and Sphingobacterium faecium were abundant and the underlying strains were successfully isolated. Interestingly, Klebsiella variicola (OTU1062) was found to dominate in both consortia, whereas K. variicola-affiliated strains retrieved from untreated wheat straw consortia showed endoglucanase/xylanase activities. Among the fungal players with high biotechnological relevance, we recovered members of the genera Penicillium, Acremonium, Coniochaeta and Trichosporon. Remarkably, the presence of peroxidases, alpha-L-fucosidases, beta-xylosidases, beta-mannases and beta-glucosidases, involved in lignocellulose degradation, was indicated by predictive bacterial metagenome reconstruction. Reassuringly, tests for specific (hemi)cellulolytic enzymatic activities, performed on the consortial secretomes, confirmed the presence of such gene functions.ConclusionIn an in-depth characterization of two wheat straw degrading microbial consortia, we revealed the enrichment and selection of specific bacterial and fungal taxa that were presumably involved in (hemi) cellulose degradation. Interestingly, the microbial community composition was strongly influenced by the wheat straw pretreatment. Finally, the functional bacterial-metagenome prediction and the evaluation of enzymatic activities (at the consortial secretomes) revealed the presence and enrichment of proteins involved in the deconstruction of plant biomass.

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Section: Discussionmentioning

confidence: 99%

Metataxonomic profiling and prediction of functional behaviour of wheat straw degrading microbial consortia

Jiménez

Dini‐Andreote

Elsas

2014

Biotechnol Biofuels

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“…Like other flavin carbohydrate oxidases that target the hydroxyl group of the anomeric carbon, GOOX-T1 is thought to mediate oxidoreductase activity through two half-reactions: 1) oxidation of the reducing sugar to the corresponding lactone, and 2) reduction of molecular oxygen to hydrogen peroxide [11]. Subsequent hydrolysis of the lactone product to the corresponding carboxylic acid may then occur.…”

Section: Introductionmentioning

confidence: 99%

Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictumand variants with reduced substrate inhibition

Vuong

Vesterinen

Foumani

et al. 2013

Biotechnol Biofuels

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BackgroundThe oxidation of carbohydrates from lignocellulose can facilitate the synthesis of new biopolymers and biochemicals, and also reduce sugar metabolism by lignocellulolytic microorganisms, reserving aldonates for fermentation to biofuels. Although oxidoreductases that oxidize cellulosic hydrolysates have been well characterized, none have been reported to oxidize substituted or branched xylo-oligosaccharides. Moreover, this is the first report that identifies amino acid substitutions leading to GOOX variants with reduced substrate inhibition.ResultsThe recombinant wild type gluco-oligosaccharide oxidase (GOOX) from the fungus Sarocladium strictum, along with variants that were generated by site-directed mutagenesis, retained the FAD cofactor, and showed high activity on cello-oligosaccharide and xylo-oligosaccharides, including substituted and branched xylo-oligosaccharides. Mass spectrometric analyses confirmed that GOOX introduces one oxygen atom to oxidized products, and 1H NMR and tandem mass spectrometry analysis confirmed that oxidation was restricted to the anomeric carbon. The A38V mutation, which is close to a predicted divalent ion-binding site in the FAD-binding domain of GOOX but 30 Å away from the active site, significantly increased the kcat and catalytic efficiency of the enzyme on all oligosaccharides. Eight amino acid substitutions were separately introduced to the substrate-binding domain of GOOX-VN (at positions Y72, E247, W351, Q353 and Q384). In all cases, the Km of the enzyme variant was higher than that of GOOX, supporting the role of corresponding residues in substrate binding. Most notably, W351A increased Km values by up to two orders of magnitude while also increasing kcat up to 3-fold on cello- and xylo-oligosaccharides and showing no substrate inhibition.ConclusionsThis study provides further evidence that S. strictum GOOX has broader substrate specificity than the enzyme name implies, and that substrate inhibition can be reduced by removing aromatic side chains in the -2 binding subsite. Of the enzyme variants, W351A might be particularly advantageous when oxidizing oligosaccharides present at high substrate concentrations often experienced in industrial processes.

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“…Most of them are of eukaryotic origin, which can make efficient overexpression of the AO encoding genes a tedious task. AOs can also act on a wide range of compounds like carbohydrates, [5] aliphatic alcohols, [6] aromatic alcohols [7] and steroids. [8] However, their use for synthetic purposes is still limited when compared to the extensive number of oxidase-based biosensing and diagnostic applications.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Biocatalytic Scope of Alditol Oxidase from Streptomyces coelicolor

et al. 2009

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Abstract:The substrate scope of the flavoprotein alditol oxidase (AldO) from Streptomyces coelicolor A3(2), recombinantly produced in Escherichia coli, was explored. While it has been established that AldO efficiently oxidizes alditols to d-aldoses, this study revealed that the enzyme is also active with a broad range of aliphatic and aromatic alcohols. Alcohols containing hydroxy groups at the C-1 and C-2 positions like 1,2,4-butanetriol (K m = 170 mM, k cat = 4.4 s À1 ), 1,2-pentanediol (K m = 52 mM, k cat = 0.85 s À1) and 1,2-hexanediol (K m = 97 mM, k cat = 2.0 s À1 ) were readily accepted by AldO. Furthermore, the enzyme was highly enantioselective for the oxidation of 1,2-diols [e.g., for 1-phenyl-1,2-ethanediol the (R)-enantiomer was preferred with an E-value of 74]. For several diols the oxidation products were determined by GC-MS and NMR. Interestingly, for all tested 1,2-diols the products were found to be the a-hydroxy acids instead of the expected a-hydroxy aldehydes. Incubation of (R)-1-phenyl-1,2-ethanediol with O) revealed that a second enzymatic oxidation step occurs via the hydrate product intermediate. The relaxed substrate specificity, excellent enantioselectivity, and independence of coenzymes make AldO an attractive enzyme for the preparation of optically pure 1,2-diols and a-hydroxy acids.

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Occurrence and Biocatalytic Potential of Carbohydrate Oxidases

Cited by 94 publications

References 160 publications

Metataxonomic profiling and prediction of functional behaviour of wheat straw degrading microbial consortia

Metataxonomic profiling and prediction of functional behaviour of wheat straw degrading microbial consortia

Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictumand variants with reduced substrate inhibition

Exploring the Biocatalytic Scope of Alditol Oxidase from Streptomyces coelicolor

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