Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae correlates with an increased association with immunoglobulin heavy-chain binding protein (BiP)

Article Abstract:

Research was performed to identify the cause of the low level of secretion of a hydrophobic mutant cutinase by Saccharomyces cerevisiae using pulse-chase experiments, immunogold labelling and electron microscopy. Results revealed a colocalization of hydrophobic mutant cutinase with immunoglobulin heavy-chain binding protein (BiP) in the endoplasmic reticulum. Furthermore, wild-type cutinase expression did not lead to higher levels of molecular chaperone BiP but BiP levels were heightened by increased induction of the hydrophobic mutant cutinase.

Carrier proteins, Transport proteins, Immunoglobulins

Expression and secretion of defined cutinase variants by Aspergillus awamori

Article Abstract:

Research was conducted to determine whether the cutinase variants from Fusariium solani pisi can be expressed successfully by the filamentous fungus Aspergillus awamori. Results demonstrate rapid extracellular degradation of cutinase occurred due to the single L51S substitution. The overexpression of the A. awamori gene encoding the chaperone BiP in the cutinase-producing A. awamori strains had no substantial impact on the secretion efficiency of the cutinases.

Genetic aspects, Aspergillus, Secretion, Gene expression, Mutagenesis, Fusarium

Introduction of an N-glycosylation site increases secretion of heterologous proteins in yeasts

Article Abstract:

Researchers were able to increase the secretion of an enzyme by Saccharomyces cerevisiae five-fold by putting an N-glycosylation consensus sequence in the N-terminal region. This technique could be used to enhance the preferential secretion of a particular protein for industrial purposes.

Microbial genetic engineering, Industrial microbiology