Apr 17, 2020

Insights into structure of Penicillium funiculosum LPMO and its synergistic saccharification performance with CBH1 on high substrate loading upon simultaneous overexpression

BioRxiv : the Preprint Server for Biology
O. A. OgunyewoSyed Shams Yazdani

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are crucial industrial enzymes required in the biorefinery industry as well as in natural carbon cycle. These enzymes known to possess auxiliary activity are produced by numerous bacterial and fungal species to assist in the degradation of cellulosic biomass. In this study, we annotated and performed structural analysis of an uncharacterized thermostable LPMO from Penicillium funiculosum(PfLPMO9) in an attempt to understand nature of this enzyme in biomass degradation. PfLPMO9 exhibited 75% and 36% structural identity to Thermoascus aurantiacus (TaLPMO9A) and Lentinus similis (LsLPMO9A), respectively. Analysis of the molecular interactions during substrate binding revealed that PfLPMO9 demonstrated a higher binding affinity with a {Delta}G free energy of -46 k kcal/molwhen compared with that of TaLPMO9A (-31 kcal/mol). The enzyme was further found to be highly thermostable at elevated temperature with a half-life of ~88 h at 50 oC. Furthermore, multiple fungal genetic manipulation tools were employed to simultaneously overexpress this LPMO and Cellobiohydrolase I (CBH1) in catabolite derepressed strain of Penicillium funiculosum, Pf Mig188, in order to improve its saccharification per...Continue Reading

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Biological Markers
Meiotic Cell Cycle
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Body Part
genetic element
Genome
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Cleaved
Gibberella moniliformis
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