Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution

Olga V. Moroz, Elena Blagova, Edward Taylor, Johan P. Turkenburg, Lars K. Skov, Garry P. Gippert, Kirk M. Schnorr, Li Ming, Liu Ye, Mikkel Klausen, Marianne T. Cohn, Esben G.W. Schmidt, Søren Nymand-Grarup, Gideon J. Davies, Keith S. Wilson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Muramidases/lysozymes hydrolyse the peptidoglycan component of the bacterial cell wall. They are found in many of the glycoside hydrolase (GH) families. Family GH25 contains muramidases/lysozymes, known as CH type lysozymes, as they were initially discovered in the Chalaropsis species of fungus. The characterized enzymes from GH25 exhibit both β-1,4-N-acetyl- and β-1,4-N,6-O-diacetylmuramidase activities, cleaving the β-1,4-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) moieties in the carbohydrate backbone of bacterial peptidoglycan. Here, a set of fungal GH25 muramidases were identified from a sequence search, cloned and expressed and screened for their ability to digest bacterial peptidoglycan, to be used in a commercial application in chicken feed. The screen identified the enzyme from Acremonium alcalophilum JCM 736 as a suitable candidate for this purpose and its relevant biochemical and biophysical and properties are described. We report the crystal structure of the A. alcalophilum enzyme at atomic, 0.78 Å resolution, together with that of its homologue from Trichobolus zukalii at 1.4 Å, and compare these with the structures of homologues. GH25 enzymes offer a new solution in animal feed applications such as for processing bacterial debris in the animal gut.

Original languageEnglish
Article numbere0248190
JournalPLoS ONE
Publication statusPublished - 12 Mar 2021

Bibliographical note

© 2021 Moroz et al.

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