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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.
Original languageEnglish
JournalCarbohydrate Research
Volume449
Pages (from-to)85-94
ISSN0008-6215
DOIs
StatePublished - 2017
CitationsWeb of Science® Times Cited: 1

    Keywords

  • Aspergillus fumigatus, Aspergillus terreus, Cellulose hydrolysis, Chaetosartorya cremea, Lytic polysaccharide monooxygenase, Malbranchea cinamomea, Myceliophthora thermophila, Penicillium citrinum, Soy polysaccharides, Soy spent flake, Talaromyces leycettanus, Trichoderma reesei
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