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

ABSTRACT: Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activi

SUBMITTER: Bonzom C 

PROVIDER: S-EPMC6691016 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature