Portal de Periódicos da CAPES

Structural Characterization of N‐Linked Oligosaccharides from Cellobiohydrolase I Secreted by the Filamentous Fungus Trichoderma Reesei RUTC 30

1997; Wiley; Volume: 245; Issue: 3 Linguagem: Inglês

10.1111/j.1432-1033.1997.00617.x

1432-1033

Marleen Maras, A. De Bruyn, Jan Schraml, Piet Herdewijn, Marc Claeyssens, Walter Fiers, Roland Contreras,

Microbial Metabolites in Food Biotechnology

We have characterized the primary structures of the predominant N‐linked oligosaccharides on cellobiohydrolase I from the filamentous fungus Trichoderma reesei RUTC30. Different enzymatic and chro‐matographic techniques were used to analyze six oligosaccharides. The combined data showed that the fungal carbohydrates have a core structure that is identical to the mammalian N‐linked core. In the bulk of the N‐glycans, the α‐1,3 arm is extended with two mannoses and a glucose, suggesting incomplete processing of the oligosaccharides in the endoplasmic reticulum. The α‐1,6 arm shows a remarkable heterogeneity: in addition to α‐1,2‐Man and α‐1,6‐Man, the presence of a terminal mannose a‐1,6‐phos‐phodiester was observed. This latter substituent has not been characterized before on mannosidase‐processed N‐glycan and its function and synthesis pathway are entirely unknown. The predominant N‐glycans on cellobiohydrolase I can be represented as follows: GlcMan 8 GIcNAc 2 , GlcMan 7 GlcNAc 2 , ManGlcNAc 2 , ManPGlcMan 7 GlcNAc 2 , GlcMan 5 GlcNAc 2 , and Man 5 GlcNAc 2 .