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Fig. 6 | Journal of Biological Engineering

Fig. 6

From: Unique N-glycosylation of a recombinant exo-inulinase from Kluyveromyces cicerisporus and its effect on enzymatic activity and thermostability

Fig. 6

Purification, glycan sites and specific enzyme activity analysis of the mutants with altered N-glycosylation modification. a, SDS-PAGE analysis of the purified wild-type rKcINU1 and its mutants. Lane M: the protein marker; Lane 1: the purified rKcINU1; Lane 2: the purified N362Q; Lane 3: the purified N370Q; Lane 4: the purified N399Q; Lane 5: the purified N467Q; Lane 6: the purified N526Q; Lane 7: the purified Mut. b, the 3D model of Mut with six novel N-glycosylation sites completely different from the wild-type. The six new glycosylation sites (Asn-9, Asn-147, Asn-153, Asn-197, Asn-203, Asn-232) as indicated by sticks were all located at the N-terminal catalytic region instead of the C-terminal domain. Its catalytic active sites (Asp-30, Asp-159 and Glu-215) were indicated by sticks in purple. c, the relative specific enzyme activity of mutants. The value given represented the average of three replications, and the specific activity of the wild-type was designated as 100%. * P < 0.01

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