Heterologous expression of glucose oxidase in the yeast Kluyveromyces marxianus.

ABSTRACT:

Background

In spite of its advantageous physiological properties for bioprocess applications, the use of the yeast Kluyveromyces marxianus as a host for heterologous protein production has been very limited, in constrast to its close relative Kluyveromyces lactis. In the present work, the model protein glucose oxidase (GOX) from Aspergillus niger was cloned into K. marxianus CBS 6556 and into K. lactis CBS 2359 using three different expression systems. We aimed at verifying how each expression system would affect protein expression, secretion/localization, post-translational modification, and biochemical properties.

Results

The highest GOX expression levels (1552 units of secreted protein per gram dry cell weight) were achieved using an episomal system, in which the INU1 pro

SUBMITTER: Rocha SN 

PROVIDER: S-EPMC2817671 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature