Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126

Niderhaus, Cecilia; Garrido, Mercedes María; Insani, Marina; Campos, Eleonora; Wirth, Sonia

doi:10.1016/j.procbio.2018.01.017

Cited by 20 publications

(12 citation statements)

References 48 publications

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“…Indeed, the reaction allows the transfer of oligosaccharide moieties onto an acceptor in a single catalytic step and provides the means to synthesise oligosaccharides of high degrees of polymerisation (DP) >10. Endo ‐1,4‐β‐xylanase is the predominant enzyme class in the GH10 family and the subject of numerous studies [59–62] . Both negative and positive subsites [24] in GH10 xylanases have been probed to understand their influence on substrate binding and catalysis, [63–66] including those in Rm Xyn10A_CM [58] .…”

Section: Resultsmentioning

confidence: 99%

Rational Enzyme Design without Structural Knowledge: A Sequence‐Based Approach for Efficient Generation of Transglycosylases

Tezé

Zhao

Wiemann

et al. 2021

Chemistry A European J

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Glycobiology is dogged by the relative scarcity of synthetic, defined oligosaccharides. Enzyme-catalysed glycosylation using glycoside hydrolases is feasible but is hampered by the innate hydrolytic activity of these enzymes. Protein engineering is useful to remedy this, but it usually requires prior structural knowledge of the target enzyme, and/or relies on extensive, time-consuming screening and analysis. Here, a straightforward strategy that involves rational rapid in silico analysis of protein sequences is described. The method pinpoints 6-12 single-mutant candidates to improve transglycosylation yields. Requiring very little prior knowledge of the target enzyme other than its sequence, the method is generic and procures catalysts for the formation of glycosidic bonds involving various d/l-, α/β-pyranosides or furanosides, and exo or endo action. Moreover, mutations validated in one enzyme can be transposed to others, even distantly related enzymes.

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Section: Resultsmentioning

confidence: 99%

Rational Enzyme Design without Structural Knowledge: A Sequence‐Based Approach for Efficient Generation of Transglycosylases

Tezé

Zhao

Wiemann

et al. 2021

Chemistry A European J

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show abstract

“…This is because the reaction allows the transfer of oligosaccharide moieties onto an acceptor in a single catalytic step and provides the means to synthesize higher oligosaccharides displaying degrees of polymerisation (DP) > 10. Endo-1,4β-xylanase is the predominant enzyme class in the GH10 family and the subject of numerous studies [38][39][40][41] . Both negative and positive subsites 23 in GH10 xylanases have been probed to understand their influence on substrate binding and catalysis [42][43][44][45] , including RmXyn10A─CM, the catalytic module of the endo-xylanase from Rhodothermus marinus used here 46 .…”

mentioning

confidence: 99%

Rational Enzyme Design Without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Glycosylation Catalysts

Tezé

Zhao

Wiemann³

et al. 2020

Preprint

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“…The coding sequence of laccase CotA was amplified from total DNA ofBacillus subtilis ATCC 6633 using oligonucleotides CotFw (5 -GGATCCATATGACACTTGAAAAATTTG-3 ) and CotRv (5 -AAGCTTATTTATGGGGATCAGTTATATC-3 ) and cloned into plasmid pGEMT-easy (Promega) for sequencing (Macrogen Korea). For CotA expression, coding sequence was cloned into vector pPICNHIS (Niderhaus et al, 2018), a derivative of plasmid pPIC9 (Invitrogen Life Technologies) in restriction sites Eco-RI/AvrII to obtain vector pPICNHISCotA (Fig. S1a).…”

Section: Production Of Recombinant Laccasesmentioning

confidence: 99%

Phenothiazines as efficient redox mediators for dye-decolorization at neutral / alkaline pH by bacterial laccases

Coria-Oriundo¹,

Battaglini²,

Wirth³

2020

Preprint

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Laccases are oxidoreductases with the outstanding ability to oxidize phenolic and non-phenolic substrates coupled to the reduction of O2 to H2O. Among them, bacterial enzymes are suitable biocatalysts for application in industrial processes under harsh conditions. However, to be active on high redox potential substrates, bacterial laccases requires of redox mediators: electron carriers between the laccase and other compounds not directly oxidizable by the enzyme. Here we demonstrate that β-(10-phenothiazyl)-propionic acid can be used as an efficient and low-cost redox mediator for decolorization of synthetic dyes by bacterial laccases. Using this laccase-mediator system, more than 80% of Indigo Carmine and Malachite Green decolorization was reached after 1 h or 2 h of incubation, respectively, both at pH 8 and in tap water (pH 6.8). Furthermore, more than 40% of Remazol Brilliant Blue R and 80% of Xylidine ponceau were decolorized after 5 h at pH 8 and 50°C. In addition, we showed this system supports at least 3 decoloration cycles without loss of activity, representing a promising biological process for cost-effective and environmentally friendly decolorization and degradation of synthetic dyes and for other industrial applications of laccases requiring neutral or alkaline pH.

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Heterologous production and characterization of a thermostable GH10 family endo-xylanase from Pycnoporus sanguineus BAFC 2126

Cited by 20 publications

References 48 publications

Rational Enzyme Design without Structural Knowledge: A Sequence‐Based Approach for Efficient Generation of Transglycosylases

Rational Enzyme Design without Structural Knowledge: A Sequence‐Based Approach for Efficient Generation of Transglycosylases

Rational Enzyme Design Without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Glycosylation Catalysts

Phenothiazines as efficient redox mediators for dye-decolorization at neutral / alkaline pH by bacterial laccases

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