TY - JOUR
T1 - Fungal GH25 muramidases
T2 - New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution
AU - Moroz, Olga V.
AU - Blagova, Elena
AU - Taylor, Edward
AU - Turkenburg, Johan P.
AU - Skov, Lars K.
AU - Gippert, Garry P.
AU - Schnorr, Kirk M.
AU - Ming, Li
AU - Ye, Liu
AU - Klausen, Mikkel
AU - Cohn, Marianne T.
AU - Schmidt, Esben G.W.
AU - Nymand-Grarup, Søren
AU - Davies, Gideon J.
AU - Wilson, Keith S.
N1 - © 2021 Moroz et al.
PY - 2021/3/12
Y1 - 2021/3/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85102617642&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0248190
DO - 10.1371/journal.pone.0248190
M3 - Article
AN - SCOPUS:85102617642
SN - 1932-6203
VL - 16
JO - PLoS ONE
JF - PLoS ONE
M1 - e0248190
ER -