Table III.

Enzymatic activity toward dabsylated glycopeptide carrying an biantennary N-glycan with two terminal β-GalNAc residues

Enzyme	% βGNβGN	% βGNGn or % GnβGN	% GnGn or % βGNM or % MβGN	% GnM or MGn	% MM
No enzyme control	100.0	0.0	0.0	0.0	0.0
DmFDLa	100.0	0.0	0.0	0.0	0.0
DmFDLb	29.9	54.3	15.8	0.0	0.0
AmFDLa	97.4	0.0	2.6	0.0	0.0
AmFDLb	2.1	3.8	18.5	75.6	0.0
CeHEX-2	0.0	0.0	0.0	23.1	76.9
CeHEX-3	0.0	0.0	0.0	100.0	0.0
CeHEX-4	0.0	0.0	100.0	0.0	0.0
JB hexosaminidase	0.7	0.0	10.4	0.5	88.5

Incubations were performed for 16 h. The product formation was quantified by estimating the area of the detected peaks in MALDI-TOF/TOF MS spectra. The corresponding structures of the tested substrates are shown in Figure 5A. JB, jack bean.

^aEnzymes produced in P. pastoris.

^bEnzymes produced in Trichoplusia ni Hi5 cells.