Secretion of a low and high molecular weight β-glycosidase by Yarrowia lipolytica.

ABSTRACT:

Background

The secretory production of recombinant proteins in yeast simplifies isolation and purification but also faces possible complications due to the complexity of the secretory pathway. Therefore, correct folding, maturation and intracellular transport of the recombinant proteins are important processing steps with a higher effort needed for complex and large proteins. The aim of this study was to elucidate the secretion potential of Yarrowia lipolytica for low and high molecular weight β-glycosidases in a comparative cultivation approach.

Results

A low sized β-glucosidase from Pyrococcus furiosus (CelB; 55 kDa) and a large sized β-galactosidase isolated from the metagenome (M1; 120 kDa) were integrated into the acid extracellular protease locus using the CRISPR-Cas9

SUBMITTER: Swietalski P 

PROVIDER: S-EPMC7216700 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature