Centre Technology Transfer CITTRU

Chitinase A – potential applications in various fields.

Posted by Centre Technology Transfer CITTRUResponsive · Patents for licensing · Poland

Summary of the technology

Methods of chitinase purification, used so far, consisted of multi-stage and expensive procedures. Affinity chromatography was also used with so-called affinity tags. These tags could interfere with the functions of chitinase, and their cut-off was associated with the next step of digestion and purification.
The proposed method of Jagiellonian University’s chitinase A purification using affinity chromatography with the involvement of G proteins is fast and efficient single-step. In addition, use of direct conjuction of chitinase and protein G eliminates the need of chitinase tagging, which may disturb protein functions, whereas their cutting requires additional digesting and purifying stage.

Centre Technology Transfer CITTRU

EN245_JU_chitinase.pdf [PDF]New and innovative aspects

Affinity chromatography exploits the ability of proteins to specific bonds, in this case, chitinase A and protein G. This protein is derived from bacterial cell walls of the genus Streptococcus and it is now commonly used in affinity. This protein complex of chitinase A with protein-G is dissociated in aqueous solution with a low pH. This allows to extract chitinase A. What is important, an acidic environment does not affect the functionality of chitinase. Chitinase retains high biological activity even at pH=2.

The new invention of the Jagiellonian University is providing a new method of chitinase A purification by affinity chromatography.

Main advantages of its use

Methods of chitinase purification, used so far, consisted of multi-stage and expensive procedures. Affinity chromatography was also used with so-called affinity tags. These tags could interfere with the functions of chitinase, and their cut-off was associated with the next step of digestion and purification.

The proposed method of Jagiellonian University’s chitinase A purification using affinity chromatography with the involvement of G proteins is fast and efficient single-step. In addition, use of direct conjuction of chitinase and protein G eliminates the need of chitinase tagging, which may disturb protein functions, whereas their cutting requires additional digesting and purifying stage. 

Specifications

Chitinases are proteins, that are found in different organisms such as viruses, bacteria, plants, insects, and mammals. They are responsible for the hydrolysis of chitin, which builds, inter alia, external skeletons of insects, arachnids, crustaceans, cell walls of fungi, algae, bacteria. Chitinases have been drawing a continuously increasing attention due to their potential use in multiple industrial sectors. The perspective of chitinase application as the environment-friendly bioinsecticide would enable replacement of chemical pesticides commonly used in agriculture. This enzyme may be also potentially used for oligosaccharide (chitin derivatives) production. These compounds may be potentially applied in food processing as natural preservatives as well as in pharmaceutical industry as, among others, germicides and fungicides, or as cholesterol reducers (chitosan derivatives).

The prevalence of the described compounds is one of the strengths of the present invention. The present invention describes an application of chitinase A, which belongs to the family Baculoviridae. The proposed method of Jagiellonian University’s chitinase A purification using affinity chromatography with the involvement of G proteins is fast and efficient single-step. In addition, use of direct conjuction of chitinase and protein G eliminates the need of chitinase tagging, which may disturb protein functions, whereas their cutting requires additional digesting and purifying stage. 

Applications

  • agriculture as an environmentally friendly bioinsecticide, replacing pesticides;
  • food processing as a natural preservative;
  • pharmaceutical industry as a formulation of a bactericide and fungicide;
  • pharmaceutical industry as potential cholesterol‐lowering agents;
  • the energy industry with the acquisition of new, alternative and renewable energy.

Intellectual property status

New method of chitinase A purification by affinity chromatography is the subject of patent application (PCT patent application – September 2015, priority date November 2014).

Current development status

Working prototype or samples ready for testing.

Desired business relationship

- commercial agreement

- licence aggreement

- technical cooperation – further development

- technical cooperation – adaptation to specific needs

Related keywords

  • Biochemistry / Biophysics Technology
  • Cellular and Molecular Biology Market
  • Molecular design Market
  • Enzymology/Protein Engineering/Fermentation
  • Alternative Energy
  • Food and Beverages
  • chitinase a
  • Enzyme
  • agriculture
  • pharmaceuticals
  • food processing
  • renewable energy sources

About Centre Technology Transfer CITTRU

Technology Transfer Office from Poland

Centre for Innovation, Technology Transfer and University Development (CITTRU) is a part of Jagiellonian University, whose role is to promote university research, to support innovation and to create cooperation with the business. CITTRU main task is to offer the scientific achievements of the Jagiellonian University in the market by providing legal protection, licensing, sale of intellectual property rights, creation of academic business, coordination of company-ordered research projects, etc. Currently promoted technologies are mainly focused on new materials science, pharmacology and medical technology. Inventions offered by Jagiellonian University are promoted and awarded during numerous exhibitions, e.g. 58th International Exhibition of Innovation, Research and New Technologies INNOVA (BRUSSELS 2009), 38th International Exhibition of Invention New Techniques & Products (Geneva 2010) or 24th International exhibition of environmental equipment, technologies and services POLLUTEC (Paris 2009).

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