MOESM1 of Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila

Cyrielle Bonzom, Silvia Hüttner, Ekaterina Mirgorodskaya, Sun-Li Chong, Stefan Uthoff, Alexander Steinbüchel, Raymond Verhaert, Lisbeth Olsson
2019 Figshare  
Additional file 1. Figure S1 Examples of MS/MS spectra for an N-glycopeptide Table S1. Relative glycoform distribution for Asn179 (NQT). Table S2. Relative glycoform distribution for Asn117 (NYT) Figure S2 Enzyme kinetics for the three MtFae1a versions. Figure S3. Data points and fitting curves used during non-linear regression for calculations of the melting temperature. Figure S4. Visualization of the amino acids forming the catalytic triad and of the two glycosylated asparagine residues on a
more » ... homology model. Table S3. Estimated relative distribution (%) of glycosylation site occupancy for the two glycosylated MtFae1a preparations Figure S5 pH-dependent activity profiles of the three MtFae1a versions. Figure S6. Residual activities of the three MtFae1a versions incubated at various pHs. Table S4. Specific activities of the three immobilized MtFae1a versions depending on the immobilization pH. Figure S7. pH-dependent activity profiles of the immobilized MtFae1a versions.
doi:10.6084/m9.figshare.9565823.v1 fatcat:dmqm7q6vzjgapp5ezmmxj76g3a