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Método de degradación de proteínas para limpiar tejidos, superficies y equipos


Oferta Tecnológica
Un instituto de investigación esloveno ha desarrollado un método eficiente para la degradación de proteínas, agregados y depósitos de proteínas mediante el uso de una serina proteasa térmicamente estable. El método se aplica en la esterilización de equipos quirúrgicos en hospitales, limpieza de tejidos y protocolos de biología molecular, y es eficiente en un amplio rango de temperaturas y valores de pH y en presencia de detergentes. El instituto de investigación busca socios, como fabricantes de detergentes, con el fin de establecer acuerdos de licencia o cooperación técnica.


Protein degradation method for cleaning of textiles, surfaces, and equipment
A Slovenian research institute has developed an efficient method for degradation of proteins, proteins aggregates and deposits by using a thermally stable serine protease. The method is applicable for sterilization of surgical equipment in hospitals, cleaning of textiles, and in molecular biology protocols, and is efficient in a broad range of temperatures, pH values, and in presence of detergents. The researchers seek license or technical cooperation agreements.
Hospital equipment and surfaces contaminated with prions represent a constant health risk since prion proteins are notoriously resistant to high temperature and aggressive detergent treatments, making it difficult to sterilize such equipment using standard procedures. Moreover, there is no effective way to clean protein films in water pipes. There is need of a new, efficient, and environmentally friendly way of inactivation, elimination, and/or degradation of prion proteins. Currently used methods for prion degradation include application of extreme conditions.

The core of the invention solves these problems by introducing a simple and efficient protein degradation method using a thermally stable protease pernisine, obtained from the organism Aeropyrum pernix. The invention further includes a procedure in which pernisine is produced (expressed) in a common laboratory bacterium Escherichia coli (E. coli), and the protein gene sequence is specifically modified to allow for higher yields. The recombinant pernisine, purified from the lysed culture supernatant, is effective against soluble proteins as well as protein deposits.

Recombinant pernisines may be used (i) as replacement of proteinase K in molecular biology purification protocols (including kits); (ii) for sterilization of surgical equipment in hospitals; (iii) for cleaning of textiles (as component of washing powders and detergents); (iv) for removing allergenic peptides in food industry, or (v) for cleaning of solid surfaces with protein deposits (water pipes, bioreactor walls, etc.).

Since the technology aims to reach its full potential in cleaning products, industrial partners, such as detergent producers, are sought. Technical cooperation is sought in order to facilitate continuous development rather than just routine production. License agreements and / or agreements for technical cooperation will enable the researchers to maintain their focus on the research behind the technology whereas up-scaling to industrial level will be carried out in the industrial partner´s setting.

The researchers are among the leading scientists in their respective departments, and regularly publish in high-impact scientific journals. They are experts in the field of protein chemistry and biochemistry, extraction, purification, and isolation of proteins from thermophilic microorganisms, and protein stability studies.
Advantages and Innovations:
Pernisine activity has been known for over a decade, yet the procedure for its mass production has remained a challenge, not least due to extreme cultivation conditions required for the thermophilic producer. The present invention includes specifically modified pernisine gene sequences that can be transferred into a common laboratory organism (E. coli). Specific substitutions in the pernisine gene maximize pernisine production through optimized codon usage in the new host organism. Any expression vectors, suitable for use in E. coli, may be used for gene transfer, and they may reproduce autonomously or in the host´s chromosome. The recombinant pernisine may be further modified (e. g. by histidine additions) for the purpose of easier purification and detection, and/or to improve solubility.

The advantages of the technology are as follows: (i) pernisine degrades protein aggregates rapidly compared to other enzymes (in less than 10 min) and is much more effective than the commonly used proteinase K; (ii) high efficiency allows for degradation of higher concentrations of contaminants; (iii) pernisine is thermally stable and efficient in a broad temperature range (50-125°C); (iv) pernsine is robust, it works in a wide pH range (3-10) and in presence of detergents and other denaturants (urea, gvanidinium hydrochloride...); (v) pernisine is environmentally friendly compared to aggressive chemical agents; (vi) pernisine may be used in combination with detergents; (vii) expression in E. coli eliminates the need for extreme cultivation conditions; (viii) expression in E. coli leads to higher yields (and in shorter time) compared to A. pernix; and (ix) specific modifications allow for simple purification and detection of pernisine.
Stage of Development:
Under development/lab tested
Patent(s) applied for but not yet granted,Patents granted

Partner sought

Type and Role of Partner Sought:
- Type of partner sought: Industry, academy, research organisation,

- Specific area of activity of the partner: distribution of proteins, production of washing powders and cleaning products, sterilization of medical devices (surgical equipment)

- Task to be performed by the partner sought: licensing in the technology for the purpose of application in cleaning formulations and procedures as well as industrial-scale production; entering technical cooperation agreements for the purpose of further development of sterilization procedures and optimisation of enzyme production


Type and Size of Client:
R&D Institution
Already Engaged in Trans-National Cooperation:
Languages Spoken:


Technology Keywords:
06002004 Ingeniería de proteínas
08002002 Microbiología / toxicología / control de calidad de alimentos
03004009 Soaps, detergents
06002003 Tecnología de enzimas
03001001 Tecnologías de limpieza