Shift and synergy of multi-function activities of a novel chitinase(ChiEnl)from Coprinopsis cinerea for efficient degradation of chitin and chitin-oligosaccharides


Xin Niu;Yan-Xin Wang;Cui-Cui Liu;Zhong-Hua Liu;Sheng Yuan;


Fruiting bodies of ink mushrooms,which have a mature pileus that is completely disintegrated and liquefied by the action of various cell wall glycoside hydrolases,are a good resource for highly efficient hydrolysis enzymes.In this study,we report a novel chitinase,ChiEnl,from Coprinopsis cinerea,which contains multi-enzyme activities,including exo-N,N'-diacetylchitobiohydrolase activity,transglycosylation activity,and endochitinase activity.Notably,these three activities of ChiEnl shift relative to each other with the degree of polymerization of chitin oligosaccharides.ChiEnl released(GlcNAc)2 residues from the non-reduced end of(GlcNAc)3_5 via exo-N,N'-diacetylchitobiohydrolase activity,whereas it cleaved(GlcNAc)3 and relative chitin oligosaccharides from(GlcNAc)_(6-8)via endochitinase activity.ChiEnl also transferred a(GlcNAc)_2-residue between chitin oligosaccharides(GlcNAc)4_6,but not between(GlcNAc)3,to produce longer chitin oligosaccharides,and the latter was consequently converted to(GlcNAc)_3.Finally,(GlcNAc)_3 was degraded to(GlcNAc)_2 and GlcNAc.Interestingly,ChiEnl cleaved off(GlcNAc)_3 mainly from the non-reduced end of(GlcNAc)_8 and also degraded only colloidal chitin to(GlcNAc)_3,which was immediately split into GlcNAc and(GlcNAc)_2.We propose that although ChiEnl does not possessβ-N-acetylhexosaminidase activity,it converts chitin or chitin oligosaccharides to GlcNAc monomers via the synergistic action of its three endogenous enzyme activities.


Coprinopsis cinerea;;Chitin;;Endochitinase;;Exo-N,N'-diacetylchitobiohydrolase;;Transglycosylation


To explore the background and basis of the node document

Springer Journals Database

Total: 0 articles

Similar documents

Documents that have the similar content to the node document

Springer Journals Database

Total: 0 articles