Hydrophobin mHFBI gene, expressed protein and application

Abstract

The invention discloses a hydrophobin mHFBI gene, expressed protein and application. The nucleotide sequence of the hydrophobin mHFBI gene is shown as SEQ ID NO. 2; by using an escherichia coli expression system, cysteine in an original Trichoderma reesei HFBI gene is mutated into serine by a genetic engineering method so as to obtain the hydrophobin mHFBI gene with high expression, good expressedhydrophobin solubility and a short production cycle; experiments show that 1L of a TB culture medium can obtain 2mg of target protein mHFBI. The protein expressed by the hydrophobin mHFBI gene has amphiphilicity and application properties which are similar to those of fungal hydrophobin HFBI. The expressed protein can still be used as an emulsifier so as to enable small oil droplets to stably exist in water, and can also be used as a dispersant for dispersing graphene and carbon nanotubes so as to solve the dispersion problem of a hydrophobic material.

Description

technical field [0001] The invention belongs to the genetic engineering of protein and the research on its properties, and in particular relates to the production process and application of hydrophobin mutants. Background technique [0002] Hydrophobins are a class of small molecular weight proteins secreted by higher filamentous fungi during specific physiological periods. After research and analysis, it is found that this kind of protein has high surface activity, and can form an amphiphilic protein film at the two-phase interface through self-assembly, thereby changing the affinity / hydrophobicity of the original medium surface. Due to its special physical and chemical properties and amphiphilic Amphiphilic properties make hydrophobins, like surfactants, self-assemble at the two-phase interface to form amphiphilic protein films with nanoscale thickness. This nanoscale protein film can efficiently change the surface properties of almost any interface, enhance the hydrophil...

AI Technical Summary

Problems solved by technology

However, the cost of the isolation process is high, and it is difficult to achieve large-scale production; it has also been reported that the prokaryotic system (such as Escherichia coli) with simple operation and high expression level is used to express hydrophobin, but inclusion bodies are formed due to protein folding and modification during the expression process. Furthermore, the denaturation and renaturation operations of inclusion bodies are involved, which further increases the production cost and the production cycle, making the large-scale production and purification of hydrophobin difficult.

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