The Functional Characterization of an AA10 Lytic Polysaccharide Monooxygenase from Saccharophagus degradans 2-40T for Enhanced Chitin Biodegradation

Lytic polysaccharide monooxygenases (LPMOs) represent copper-dependent enzymes pivotal in breaking down resilient polysaccharides like cellulose and chitin by means of oxidation, creating more accessible sites for glycoside hydrolases. To elevate the conversion efficiency of chitin, an AA10 LPMO was identified from the genome of <i>Saccharophagus degradans</i> 2-40^T and heterologously expressed. The optimal pH for the activity of recombinant <i>Sd</i>LPMO10A is 9.0, and the optimal temperature is 60 °C. Assessment of <i>Sd</i>LPMO10A's synergism with commercial chitinase indicated that when comparing the enzyme combination's activity to the activity of chitinase alone, the synergistic effect was significant, and a one-pot reaction appeared superior to a two-step reaction. This discovery of a functional AA10 family LPMO presents a promising avenue for developing highly efficient catalysts for biomass conversion of chitin-rich food processing waste (e.g., shrimp shells) into bioactive chitooligosaccharides with applications in functional foods, such as prebiotics and antioxidants.