Characterization of the oxidative inactivation of xylanase by laccase and a redox mediator

Bendl, Ryan F.; Kandel, Jason M.; Amodeo, Katherine D.; Ryder, Andrew M.; Woolridge, Elisa M.

doi:10.1016/j.enzmictec.2007.11.010

Cited by 14 publications

(13 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The second challenge to a mixed enzyme system application is that the LMS is known to inactivate xylanase and in some accounts even laccase itself [8,34,40,88,169]. However, xylanase inactivation can be slowed via protection by its substrate xylan; in fact, loss of xylanase activity from supernatant in heterogeneous pulp systems may be attributable to enzyme binding to fiber, not to inactivation.…”

Section: Obstaclesmentioning

confidence: 99%

“…This was demonstrated to be an active site directed process by observing saturation of the inactivation and protection by the xylanase substrate xylan [40]. Inactivation occurred as a result of tryptophan oxidation, evidenced as a decrease in protein fluorescence and identification via mass spectrometry of conversion of at least Trp17 and Trp18 to oxindolealanine residues.…”

Section: Susceptibility Of Xylanase To Oxidative Inactivationmentioning

confidence: 99%

“…In the alignment of seven family 11 xylanases shown in Figure 3, Trp19 of B. agaradhaerens, equivalent to Trp9 of B. subtilis, is conserved in all, and is also highly conserved among family 10 xylanases. Trp19 has been implicated in xylanase activity through chemical modification, leading many investigators to site the key role of tryptophan at the active site [40,99,124,[130][131][132].…”

Section: Susceptibility Of Xylanase To Oxidative Inactivationmentioning

confidence: 99%

See 2 more Smart Citations

Mixed Enzyme Systems for Delignification of Lignocellulosic Biomass

Woolridge

2014

Catalysts

View full text Add to dashboard Cite

Abstract:The application of enzymes such as laccase and xylanase for the preparation of cellulose from lignocellulosic material is an option for those industries seeking to reduce the use of chlorine-containing bleach agents, thus minimizing the environmental impact of their processes. Mixed hydrolytic and oxidative enzyme systems have been well described in the context of biopulping, and thus provide good precedent regarding effectiveness, despite the susceptibility of xylanase to inactivation by laccase-generated oxidants. This paper examines the progress towards development of sequential and simultaneous mixed enzyme systems to accomplish delignification.

show abstract

Section: Obstaclesmentioning

confidence: 99%

Section: Susceptibility Of Xylanase To Oxidative Inactivationmentioning

confidence: 99%

Section: Susceptibility Of Xylanase To Oxidative Inactivationmentioning

confidence: 99%

See 1 more Smart Citation

Mixed Enzyme Systems for Delignification of Lignocellulosic Biomass

Woolridge

2014

Catalysts

View full text Add to dashboard Cite

show abstract

“…assayed by measuring the formation of reducing sugars at 540 nm from xylan via the dinitrosalicylate method using the dinitrosalicylate reagent [19]. Laccase activity was determined by monitoring the oxidation of 5 mM 2,2´-azinobis-(3-ethylbenzthiazoline-6-sulphonate) in a 50 mM sodium acetate buffer (pH 5.0) [20].…”

Section: Key Termsmentioning

confidence: 99%

Influence of fungal pretreatment on thermogravimetric characteristics and fast pyrolysis vapors of corn stover

Wang

Zeng

et al. 2011

Biofuels

View full text Add to dashboard Cite

show abstract

“…However, they may also attack (hemi)cellulose or even (hemi)cellulases, potentially hampering industrial enzymatic (hemi)cellulose conversion [84,85]. For the peroxidases, autooxidation or inactivation may severely limit their performance.…”

Section: Lignocellulose Oxidoreductasesmentioning

confidence: 99%

Biomass Converting Enzymes as Industrial Biocatalysts for Fuels and Chemicals: Recent Developments

2012

View full text Add to dashboard Cite

Abstract:The economic utilization of abundant lignocellulosic biomass as a feedstock for the production of fuel and chemicals would represent a profound shift in industrial carbon utilization, allowing sustainable resources to substitute for, and compete with, petroleum based products. In order to exploit biomass as a source material for production of renewable compounds, it must first be broken down into constituent compounds, such as sugars, that can be more easily converted in chemical and biological processes. Lignocellulose is, unfortunately, a heterogeneous and recalcitrant material which is highly resistant to depolymerization. Many microorganisms have evolved repertoires of enzyme activities which act in tandem to decompose the various components of lignocellulosic biomass. In this review, we discuss recent advances in the understanding of these enzymes, with particular regard to those activities deemed likely to be applicable in commercialized biomass utilization processes.

show abstract

Characterization of the oxidative inactivation of xylanase by laccase and a redox mediator

Cited by 14 publications

References 42 publications

Mixed Enzyme Systems for Delignification of Lignocellulosic Biomass

Mixed Enzyme Systems for Delignification of Lignocellulosic Biomass

Influence of fungal pretreatment on thermogravimetric characteristics and fast pyrolysis vapors of corn stover

Biomass Converting Enzymes as Industrial Biocatalysts for Fuels and Chemicals: Recent Developments

Contact Info

Product

Resources

About