A highly xyloglucan active lytic polysaccharide monooxygenase EpLPMO9A from Eupenicillium parvum 4-14 shows boosting effect on hydrolysis of complex lignocellulosic substrates.

Abstract:

:The recently identified lytic polysaccharide monooxygenases (LPMOs) are important auxiliary proteins which contribute to lignocellulose biodegradation by oxidatively cleaving the glycosidic bonds in cellulose and other polysaccharides. The vast differences in terms of substrate specificity and regioselectivity within LPMOs provide us new possibilities to find promising candidates for the use in enzyme cocktails in biorefinery applications. In this study, a highly xyloglucan active family AA9 lytic polysaccharide monooxygenase EpLPMO9A was identified from Eupenicillium parvum 4-14. EpLPMO9A exhibited a mixed C1/C4 oxidative cleavage activity on cellulose and xyloglucan with a broad range of pH stability and good thermal stability at 40 °C. It showed a higher boosting effect on the enzymatic saccharification of complex lignocellulosic substrates associated with xyloglucan than on the lignocellulosic substrates without xyloglucan particularly in low commercial cellulase dosage cases. The oxidative cleavage of xyloglucan by EpLPMO9A may facilitate to open up the sterical hindrance of cellulose by xyloglucan and thereby increase accessibility for cellulase to lignocellulosic substrates. The discovery of more and more hemicellulose-active LPMOs and their contribution to breaking down the barriers by oxidatively acting on hemicellulose may expand our knowledge for their functions of LPMOs in lignocellulose biodegradation.

journal_name

Int J Biol Macromol

authors

Shi Y,Chen K,Long L,Ding S

doi

10.1016/j.ijbiomac.2020.11.177

subject

Has Abstract

pub_date

2021-01-15 00:00:00

pages

202-213

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)35102-3

journal_volume

167

pub_type

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