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Synergistic action of a lytic polysaccharide monooxygenase and a cellobiohydrolase from Penicillium funiculosum in cellulose saccharification under high substrate loading

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Title Synergistic action of a lytic polysaccharide monooxygenase and a cellobiohydrolase from Penicillium funiculosum in cellulose saccharification under high substrate loading
 
Creator Ogunyewo, Olusola A.
Randhawa, Anmoldeep
Gupta, Mayank
Kaladhar, Vemula Chandra
Verma, Praveen K.
Yazdani, Syed Shams
 
Subject fungus
lytic polysaccharide monooxygenase (LPMO)
cellulase
Penicillium funiculosum
PfMig1
cellobiohydrolase I (CBH1)
saccharification
 
Description Accepted date: 15 Sept 2020
Lytic polysaccharide monooxygenases (LPMOs) are crucial industrial enzymes required in the biorefinery industry as well as in the natural carbon cycle. These enzymes, known to catalyze oxidative cleavage of glycosidic bonds, 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 LPMO from Penicillium funiculosum (PfLPMO9) based on computational methods in an attempt to understand the behavior of this enzyme in biomass degradation. PfLPMO9 exhibited 75% and 36% sequence identity with LPMOs from Thermoascus aurantiacus (TaLPMO9A) and Lentinus similis (LsLPMO9A), respectively. Furthermore, multiple fungal genetic manipulation tools were employed to simultaneously overexpress LPMO and cellobiohydrolase I (CBH1) in a catabolite-derepressed strain of Penicillium funiculosum, PfMig188 (an engineered variant of P. funiculosum), to improve its saccharification performance toward acid-pretreated wheat straw (PWS) at 20% substrate loading. The resulting transformants showed improved LPMO and CBH1 expression at both the transcriptional and translational levels, with ∼200% and ∼66% increases in ascorbate-induced LPMO and Avicelase activities, respectively. While the secretome of PfMig88 overexpressing LPMO or CBH1 increased saccharification of PWS by 6% or 13%, respectively, over the secretome of PfMig188 at the same protein concentration, the simultaneous overexpression of these two genes led to a 20% increase in saccharification efficiency over that observed with PfMig188, which accounted for 82% saccharification of PWS under 20% substrate loading.
 
Date 2020-09-30T09:20:12Z
2020-09-30T09:20:12Z
2020
 
Type Article
 
Identifier Applied and Environmental Microbiology, 86(23): e01769-20
1098-5336
https://doi.org/10.1128/AEM.01769-20
https://aem.asm.org/content/early/2020/09/21/AEM.01769-20/article-info
http://223.31.159.10:8080/jspui/handle/123456789/1105
 
Language en_US
 
Format application/pdf
 
Publisher American Society for Microbiology