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Updated: Feb 25, 2026

Ammonia Fiber Expansion AFEX Pretreatment of Lignocellulosic Biomass
Published on: April 18, 2020
A comparative study on the activity of fungal lytic polysaccharide monooxygenases for the depolymerization of
Brian C Pierce1, Jane Wittrup Agger2, Zhenghong Zhang3
1DuPont™ Nutrition Biosciences ApS, Edwin Rahrs Vej 38 Brabrand, 8220, Denmark; Department of Chemical and Biochemical Engineering, Center for Bioprocess Engineering, Technical University of Denmark, Søltofts Plads, Building 229, Kgs. Lyngby, 2800, Denmark; DuPont™ Nutrition & Health - Protein Solutions, 4300 Duncan Ave., Saint Louis, MO, 63110, USA.
Abstract:
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes capable of the oxidative breakdown of polysaccharides. They are of industrial interest due to their ability to enhance the enzymatic depolymerization of recalcitrant substrates by glycoside hydrolases. In this paper, twenty-four lytic polysaccharide monooxygenases (LPMOs) expressed in Trichoderma reesei were evaluated for their ability to oxidize the complex polysaccharides in soybean spent flakes, an abundant and industrially relevant substrate. TrCel61A, a soy-polysaccharide-active AA9 LPMO from T. reesei, was used as a benchmark in this evaluation. In total, seven LPMOs demonstrated activity on pretreated soy spent flakes, with the products from enzymatic treatments evaluated using mass spectrometry and high performance anion exchange chromatography. The hydrolytic boosting effect of the top-performing enzymes was evaluated in combination with endoglucanase and beta-glucosidase. Two enzymes (TrCel61A and Aspte6) showed the ability to release more than 36% of the pretreated soy spent flake glucose - a greater than 75% increase over the same treatment without LPMO addition.
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