초록
<P><B>Abstract</B></P> <P>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 <I>Trichoderma reesei</I> were evaluated for their ability to oxidize the complex polysaccharides in soybean spent flakes, an abundant and industrially relevant substrate. <I>Tr</I>Cel61A, a soy-polysaccharide-active AA9 LPMO from <I>T. reesei</I>, 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 (<I>Tr</I>Cel61A 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.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Twenty-four LPMOs were investigated for activity on NaOH pretreated soy spent flake. </LI> <LI> Seven LPMOs showed activity on pretreated soy spent flake. </LI> <LI> Oxidative activity (C1, C4, and C1-C4) was determined with ESI-MS and HPAEC-PAD. </LI> <LI> Two LPMOs (<I>Tr</I>Cel61A and Aspte6) showed significant hydrolytic boosting. </LI> <LI> LPMOs boost glucose release from soy spent flakes by EG and BG by more than 75%. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>