Suchergebnisse

Expression of recombinant proteins is important for studying their biological function. Most often, the expression system of the E. coli is used for the primary description of protein properties. However, under overexpression conditions, the rate of aggregation of target proteins often exceeds the rate of proper folding, resulting in the formation of insoluble inclusion bodies. Inclusion bodies are a clear disadvantage of the E. coli expression system because they interfere with the release of target recombinant proteins. One solution to the existing problem is the use of chaperone-like proteins in vitro to refold the target protein. In this work, the recombinant protein MF3 was taken as an example of a chaperone-like protein, which increased the yield of soluble plant chitinase by 92% compared to the yield of this protein using the standard refolding procedure.

New recombinant strains of Penicillium verruculosum have been created with a high level of expression of homologous endo-β-1,4-glucanase II and heterologous phytase A A. niger, as well as heterologous endo-1,4-β-xylanase E P. canescens and phytase A A. niger, allowing to obtain highly active feed enzyme preparations (AF) capable of simultaneously signi cantly reducing viscosity non-starch polysaccharides, as well as increase the bioavailability of phosphorus and minerals of grain-based feed and, thus, increase the digestibility of nutrients of agricultural animal and poultry feed. Speci c AF activities for speci c substrates (xylanau, β-glucan, phytate) were studied, the qualitative and quantitative component composition of new AF was determined. On the basis of a new enzyme preparation containing homologous endo-β-1,4-glucanase II and heterologous phytase A A. niger, a recipient strain ∆nia D - was obtained, into which heterologous endo-1,4-β-xylanase E P. canescens was successfully cloned and, thus, a promising producer of three target enzymes was obtained simultaneously.