|Title||Distinct substrate specificities and electron-donating systems of fungal lytic polysaccharide monooxygenases|
|Author(s)||Frommhagen, Matthias; Westphal, Adrie H.; Berkel, Willem J.H. van; Kabel, Mirjam A.|
|Source||Frontiers in Microbiology 9 (2018). - ISSN 1664-302X|
Food Chemistry Group
|Publication type||Refereed Article in a scientific journal|
|Keyword(s)||C1/C4-oxidation - Electron donor - Hydrogen peroxide - LPMO - Lytic polysaccharide monooxygenase - Oxygen - Reducing agent - Substrate specificity|
Lytic polysaccharide monooxygenases (LPMOs) are powerful enzymes that oxidatively cleave glycosidic bonds in polysaccharides. The ability of these copper enzymes to boost the degradation of lignocellulose has greatly stimulated research efforts and biocatalytic applications within the biorefinery field. Initially found as oxidizing recalcitrant substrates, such as chitin and cellulose, it is now clear that LPMOs cleave a broad range of oligo- and poly-saccharides and make use of various electron-donating systems. Herein, substrate specificities and electron-donating systems of fungal LPMOs are summarized. A closer look at LPMOs as part of the fungal enzyme machinery might provide insights into their role in fungal growth and plant-pathogen interactions to further stimulate the search for novel LPMO applications.