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Updated: Mar 30, 2026

High-throughput Saccharification Assay for Lignocellulosic Materials
Published on: July 3, 2011
Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme
Brian R Scott1, Hong Zhi Huang2, Jesper Frickman3
1Biomass Enzyme Discovery, Novozymes Inc., 1445 Drew Ave, Davis, CA, 95618, USA. bsco@novozymes.com.
Objectives:
Efficient enzymatic saccharification of plant cell wall material is key to industrial processing of agricultural and forestry waste such as straw and wood chips into fuels and chemicals.
Results:
Saccharification assays were performed on steam-pretreated wheat straw under ambient and O2-deprived environments and in the absence and presence of a lytic polysaccharide monooxygenase (LPMO) and catalase. A kinetic model was used to calculate catalytic rate and first-order inactivation rate constants of the cellulases from reaction progress curves. The addition of a LPMO significantly (P < 0.01, Student's T test) enhanced the rate of glucose release from 2.8 to 6.9 h(-1) under ambient O2 conditions. However, this also significantly (P < 0.01, Student's T test) increased the rate of inactivation of the enzyme mixture, thereby reducing the performance half-life from 65 to 35 h. Decreasing O2 levels or, strikingly, the addition of catalase significantly reduced (P < 0.01, Student's T test) enzyme inactivation and, as a consequence, higher efficiency of the cellulolytic enzyme cocktail was achieved.
Conclusion:
Oxidative inactivation of commercial cellulase mixtures is a significant factor influencing the overall saccharification efficiency and the addition of catalase can be used to protect these mixtures from inactivation.
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