two potential N-glycosylated sites within the Asn-Xaa-Ser/Thr sequence are found in the phy168 phytase. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115
two potential N-glycosylated sites within the Asn-Xaa-Ser/Thr sequence are found in the phy168 phytase. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115
analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide
enzyme AppAS contains three potential sites of N-glycosylation, recombinant nontagged enzyme from Pichia pastoris strain GS115(his4) is glycosylated, deglycosylation of rAppAP is carried out using Endo H deglycosylase
in silico analysis reveals 4 potential N-glycosylation sites, Asp165,Asp200, Asp275 and Asp346, and 3 potential O-glycosylation sites, Thr185, Thr274, and Thr321, in the enzyme
the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C
seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consisted of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview
seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consists of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
enzyme from strain NRRL 3135 and recombinant enzyme from Aspergillus niger van Tieghem are 35.29% glycosylated, only N-linked oligosaccharides, released mannose residues are (alpha1-2,3,6) linked, the trisaccharide core structure is nonfucosylated, the structure of N-linked oligosaccharides ranges from (Man)5(GlcNAc)2 to (Man)10(GlcNAc)2
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
enzyme from strain NRRL 3135 and recombinant enzyme from Aspergillus niger van Tieghem are 35.29% glycosylated, only N-linked oligosaccharides, released mannose residues are (alpha1-2,3,6) linked, the trisaccharide core structure is nonfucosylated, the structure of N-linked oligosaccharides ranges from (Man)5(GlcNAc)2 to (Man)10(GlcNAc)2
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts