Aims This work aims to determine the tolerance of xylanase towards enzyme‐generated oxidative conditions, such as those produced by the peroxidase or laccase mediator systems (LMS). Methods and Results The activity of Thermomyces lanuginosus xylanase was measured after incubation with lignin peroxidase, manganese peroxidase or laccase plus various mediators. The laccase system, using mediators such as 1‐hydroxybenzotriazole and violuric acid, resulted in complete loss of xylanase activity, accompanied by an increase in the solution potential. However, an increase in solution potential alone was not sufficient to inactivate xylanase, nor was loss of xylanase activity always accompanied by a significant increase in solution potential, as observed with N‐hydroxyphthalimide as the mediator. Neither lignin peroxidase nor manganese peroxidase impacted xylanase activity; only extended treatment with elevated hydrogen peroxide concentration promoted modest xylanase activity loss. The mechanism of inactivation as determined by the tryptophan‐modifying reagent N‐bromosuccinimide (NBS) indicated that oxidation of just one of the eight tryptophan residues of T. lanuginosus xylanase would be sufficient to result in complete loss of xylanase activity, since xylanase is completely inactivated at 1 : 1 molar ratio of NBS to xylanase. Conclusions While showing tolerance to peroxidase‐based enzyme systems, T. lanuginosus xylanase is readily inactivated in the presence of the LMS. Based upon treatment with NBS as the oxidant, inactivation can be attributed to modification of a single tryptophan residue. Significance and Impact of the Study The simultaneous application of mixed hydrolytic and oxidative enzyme systems is of importance to biomass processing industries. Understanding the tolerance of xylanase to oxidative conditions will facilitate the design of reaction conditions or enzyme variants to maximize the impact of mixed enzyme systems.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
334 Leonard St
Brooklyn, NY 11211
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.