Abstract:
:Differences in glycosylation between the natural alpha-1,6 glucan-6-glucanohydrolase from Penicillium minioluteum and the heterologous protein expressed in the yeast Pichia pastoris were analyzed. Glycosylation profiling was carried out using fluorophore-assisted carbohydrate electrophoresis and amine absorption high-performance liquid chromatography (NH(2)-HPLC) in combination with matrix-assisted laser desorption-time of flight-mass spectrometry. Both microorganisms produce only oligomannosidic type structures, but the oligosaccharide population differs in both enzymes. The native enzyme has mainly short oligosaccharide chains ranging from Man(5)GlcNAc(2) to Man(9)GlcNAc(2), of which Man(8)GlcNAc(2) was the most represented oligosaccharide. The oligosaccharides linked to the protein produced in P. pastoris range from Man(7)GlcNAc(2) up to Man(14)GlcNAc(2), with Man(8)GlcNAc(2) and Man(9)GlcNAc(2) being the most abundant structures. In both enzymes the first glycosylation site (Asn(5)) is always glycosylated. However, Asn(537) and Asn(540) are only partially glycosylated in an alternate manner.
journal_name
FEMS Yeast Resjournal_title
FEMS yeast researchauthors
Betancourt LH,García R,González J,Montesino R,Quintero O,Takao T,Shimonishi Y,Cremata JAdoi
10.1111/j.1567-1364.2001.tb00026.xkeywords:
subject
Has Abstractpub_date
2001-07-01 00:00:00pages
151-60issue
2eissn
1567-1356issn
1567-1364pii
S156713560100023Xjournal_volume
1pub_type
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