Alginate Encapsulation Stabilizes Xylanase Toward the Laccase Mediator System

Xylanase, a hydrolytic enzyme, is susceptible to inactivation by the oxidative conditions generated by the laccase mediator system (LMS). Given the impetus to develop a mixed enzyme system for application in biomass processing industries, xylanase was encapsulated with either Cu 2+ - or Ca 2+ -algin...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 2023-05, Vol.195 (5), p.3311-3326
Main Authors: Lee, Annemarie A., Gervasio, Esabelle D., Hughes, Riley O., Maalouf, Alexandra A., Musso, Samantha A., Crisalli, Alicia M., Woolridge, Elisa M.
Format: Article
Language:English
Subjects:
Alginates
Alginic acid
Biochemistry
Biomass
Biotechnology
Calcium alginate
Calcium ions
Chemistry
Chemistry and Materials Science
Copper
Encapsulation
Enzymes
Hydrolysis
Inactivation
Laccase
Original Article
Polymers
Substrates
Veratraldehyde
Veratryl alcohol
Xylan
Xylanase
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Summary:Xylanase, a hydrolytic enzyme, is susceptible to inactivation by the oxidative conditions generated by the laccase mediator system (LMS). Given the impetus to develop a mixed enzyme system for application in biomass processing industries, xylanase was encapsulated with either Cu 2+ - or Ca 2+ -alginate and then exposed to the LMS with variations such as mediator type, mediator concentration, and treatment pH. Results demonstrate that alginate-encapsulated xylanase retains substantial activity (> 80%) when exposed to the LMS relative to non-encapsulated xylanase. Cu 2+ -alginate generally provided better protection than Ca 2+ -alginate for all mediators, and protection was observed even at a low pH, where the LMS is most potent. Despite encapsulation, xylanase was still capable of hydrolyzing its polymeric substrate xylan, given k cat / K m values within an order of magnitude of that for non-encapsulated xylanase. The alginate matrix does not impede the function of the oxidized mediator, since comparable V max values were observed for the conversion of veratryl alcohol to veratraldehyde by free and Cu 2+ -alginate encapsulated laccase. Overall, these results support development of a mixed enzyme system for biomass delignification and, more broadly, show potential for protecting protein function in an oxidative environment.
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-022-04296-7