Lytic polysaccharide monooxygenases (LPMOs) are a class of oxidative enzymes that play an important
role in biomass degradation by cleaving glycosidic bonds in polysaccharides. This oxidative mechanism
significantly enhances the activity of classical hydrolytic enzymes and relies on electron donors such as
GMC oxidoreductases (AA3; e.g., cellobiose dehydrogenase, CDH), small-molecule reductants, or
photosynthetic pigments.
Clonostachys rosea, a filamentous fungus with a broad ecological repertoireincluding saprotrophy
and mycoparasitismexhibits a distinctive genomic expansion of oxidative enzyme families. The
ecological and functional relevance of these expanded gene families remains poorly understood,
particularly as C. rosea is neither a prominent lignocellulose degrader nor a plant pathogen.
This project seeks to investigate the structural, functional, and ecological significance of the AA9 family
of LPMOs in C. rosea. We will examine the environmental conditions that trigger their expression and
secretion, conduct biochemical characterization of selected LPMOs, and explore their synergistic
interactions with the CDHs. This work represents a comprehensive and innovative approach to
elucidating the regulatory and functional complexity of an unusually large AA9 gene family. Our
findings will advance understanding of how non-ligninolytic fungi utilize oxidative enzymes and will
shed light on the coordinated expression and ecological integration of AA9 and AA3 enzyme systems.