Surface display of HFBI and DewA hydrophobins on Saccharomyces cerevisiae modifies tolerance to several adverse conditions and biocatalytic performance

Appl Microbiol Biotechnol. 2021 Feb;105(4):1505-1518. doi: 10.1007/s00253-021-11090-8. Epub 2021 Jan 23.

Abstract

Hydrophobins are relatively small proteins produced naturally by filamentous fungi with interesting biotechnological and biomedical applications given their self-assembly capacity, efficient adherence to natural and artificial surfaces, and to introduce modifications on the hydrophobicity/hydrophilicity of surfaces. In this work we demonstrate the efficient expression on the S. cerevisiae cell surface of class II HFBI of Trichoderma reesei and class I DewA of Aspergillus nidulans, a hydrophobin not previously exposed, using the Yeast Surface Display a-agglutinin (Aga1-Aga2) system. We show that the resulting modifications affect surface properties, and also yeast cells' resistance to several adverse conditions. The fact that viability of the engineered strains increases under heat and osmotic stress is particularly interesting. Besides, improved biocatalytic activity toward the reduction of ketone 1-phenoxypropan-2-one takes place in the reactions carried out at both 30 °C and 40 °C, within a concentration range between 0.65 and 2.5 mg/mL. These results suggest interesting potential applications for hydrophobin-exposing yeasts. KEY POINTS : • Class I hydrophobin DewA can be efficiently exposed on S. cerevisiae cell surfaces. • Yeast exposure of HFBI and DewA increases osmotic and heat resistance. • Engineered strains show modified biocatalytic behavior.

Keywords: Biocatalysis; DewA; HFBI; Hydrophobin; Stress resistance.

MeSH terms

  • Aspergillus nidulans*
  • Cell Adhesion Molecules
  • Fungal Proteins / genetics
  • Hydrophobic and Hydrophilic Interactions
  • Hypocreales
  • Imidazoles
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins* / genetics
  • Surface Properties
  • Trichoderma* / genetics

Substances

  • AGA1 protein, S cerevisiae
  • AGA2 protein, S cerevisiae
  • Cell Adhesion Molecules
  • Fungal Proteins
  • Imidazoles
  • Saccharomyces cerevisiae Proteins
  • 1-(heptafluorobutyryl)imidazole

Supplementary concepts

  • Trichoderma reesei