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

DOI: 10.1371/journal.pone.0248190 DOI Help

Authors: Olga V. Moroz (The University of York) , Elena Blagova (The University of York) , Edward Taylor (The University of York) , Johan Turkenburg (The University of York) , Lars K. Skov (Novozymes A/S) , Garry P. Gippert (Novozymes A/S) , Kirk M. Schnorr (Novozymes A/S) , Li Ming (Novozymes A/S) , Liu Ye (Novozymes A/S) , Mikkel Klausen (Novozymes A/S) , Marianne T. Cohn (Novozymes A/S) , Esben G. W. Schmidt (Novozymes A/S) , Søren Nymand-Grarup (Novozymes A/S) , Gideon J. Davies (The University of York) , Keith S. Wilson (The University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Plos One , VOL 16

State: Published (Approved)
Published: March 2021
Diamond Proposal Number(s): 13587 , 7864

Open Access Open Access

Abstract: 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.

Journal Keywords: Fungal structure; Peptidoglycans; Enzyme structure; Crystal structure; Acremonium; Bacteriophages; Glycerol; Enzymes

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography

Added On: 16/03/2021 13:31

Documents:
journal.pone.0248190.pdf

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Pathogens Structural biology Veterinary Medicine

Technical Tags:

Diffraction Macromolecular Crystallography (MX)