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Fig. 1 | Journal of Biological Engineering

Fig. 1

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

Fig. 1

Analysis of N-glycosylation modification of the exo-inulinase from K. cicerisporus CBS4857 expressed in P. pastoris X-33. a, SDS-PAGE analysis of purified rKcINU1 treated with PNGase F. Lane M: the protein maker; Lane 1: the purified rKcINU1; Lane 2: the purified rKcINU1 treated with PNGase F under the denaturing condition; Lane 3: the purified rKcINU1 treated with PNGase F under the natural condition. b, The amino acid sequence of rKcINU1 with the putative N-glycosylation sites. The Glu just following the polyhistidines at the N-terminus was designated as the first amino acid site for the mature enzyme. Eleven potential glycosylation sites were shown in yellow including Asn-9, Asn-99, Asn-100, Asn-106, Asn-153, Asn-203, Asn-267, Asn-362, Asn-370, Asn-467 and Asn-526. c, The determination of molecular mass of rKcINU1 by MALDI-TOF mass spectrometry. The arrows indicated different glycoform ensembles with variable molecular mass

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Journal of Biological Engineering

ISSN: 1754-1611