Hydrophobins are common for filamentous fungi. Since now, their role in surface hydrophobicity, fruit body formation and sporulation has been reported. Due to their ability to attach both to hydrophilic and to hydrophobic surfaces, we hypothesized that they could enhance the enzymatic degradation of polymers by creating a monolayer, which aids the enzyme to bind the polymeric substrate or they can increase the efficiency of enzyme binding in the non-covalent enzyme immobilization. In this work, we present the effects of GST-HFB4 fusion protein from Trichoderma virens on the enzyme activity both in solution and when immobilized, as a proof of concept. Our initial hypothesis was that hydrophobins from T. virens could enhance activity of enzymes used for polymer degradation. However, due to the fact that GST-HFB4 has not affected cellulases- activity in their free form, we focused on the hydrophobin-mediated immobilization of enzymes to test the hypothesis, if hydrophobins are able to bind more enzyme activity to the surface of porous glass beads. The data obtained in this thesis depicts a positive effect on the immobilizing of glucose oxidase activity on the surface of kapton membrane with HFB7-(His)6 layer. However, in order to fully understand the differences between activities of different enzymes both in solution and when immobilized, further examinations would be needed and this data could be useful for that purpose.