Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Patent
1994-09-19
1997-09-23
Marx, Irene
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
43524054, 43524046, C12N 908
Patent
active
056703570
DESCRIPTION:
BRIEF SUMMARY
This application was filed under 35 U.S.C. 371 as the national phase of PCT16892/01700, filed Sep. 16, 1992.
FIELD OF INVENTION
This invention relates to a process for the production of peroxidase enzymes from plant cell cultures, and specific isoenzymes isolated therefrom.
BACKGROUND AND PRIOR ART
Peroxidase enzymes catalyse a host of reactions in which hydrogen peroxide is a specific oxidising agent and a wide range of substrates act as electron donors. They are widely used as enzyme labelled reagents in diagnostic, e.g. ELISA, kits, and in other biologically based molecular detection systems, but also find utility in other industries, such as in paper recycling, chemical and waste water treatment, and in detergents and bleaching agents.
Peroxidase enzymes are widely distributed in nature and are produced by a wide variety of plant species. At the present time however, the chief commercial source is horseradish. In the commercial production of horseradish peroxidase (HRP) the horseradish roots are harvested and the sprouted roots are minced mechanically in water to form a starting material. From this, peroxidase is purified by a series of ammonium sulphate and ethanol precipitations. To obtain high purity enzyme, conventional chromatographic techniques are employed. Unfortunately, this process leads to large quantities of waste tissue and problems arise with dispersing of waste. Not only this but there is a significant irreversible loss of enzyme activity resulting from the precipitations with ethanol and ammonium sulphate which are used to extract the enzyme from the tissue.
In International Patent Application, Publication No. WO91/10729, plant cell suspension cultures are described which produce an extra-cellular peroxidase in high yield and which therefore provide a convenient source of peroxidase which is not subject to the foregoing recovery problems. These are suspension cultures of peroxidase producing cells of plants of the genus Acer, and especially root cell cultures of Acer pseudoplatanus.
Various other sources have been suggested in the literature for the commercial production of peroxidase. For example, radish plant cell cultures have been suggested as a source of extra-cellular peroxidase (Plant Cell, Tissue and Organ Culture, 1989, 18:321-327) but the yields and specific activity of the product enzyme are low.
It has also been suggested that calli cultured from various plant species can be used as a source for the production of peroxidase, but callus culture is inherently incapable of large scale commercial production. Such suggestions are Contained in unexamined published Japanese Patent Applications: vat deulis Makino, Stevia rebaudiana Bettoni, and Bupleurum falcatum L.); Phellodendron amurense Rupr., Oenothera lamarchiana Ser., Scopolia japonica Maxim, Lithospermum erythrorhizon Sieb et Zucc., Glycine max Merrill, and Gynastema pentaphyllum Makino);
Other items of background at1 include:
Applied Biochemistry and Biotechnology, 1990, Vol 24/25, pp 213-222, which discloses the correlation between extra-cellular peroxidase production and plant cell growth in plant cell cultures of Artemesia annua, Coleus blumei, Pisum satiuum, and Salvia officinalis and the consequential utility of extra-cellular peroxidase concentration in such cultures as an indicator of cell growth, but not as a commercial source of peroxidase enzymes;
Care Cacao The, 1985, 29(2), pp 113-120 which reports on the effects of fermentation on the activity of peroxidase and polyphenol-oxidase enzymes in the cocoa bean, but in no way suggests cell cultures of T. cacao as a commercial source of peroxidase;
Indian Journal Experimental Biology, 1983, Vol 21, pp 65-68 which reports on the role of o- and p-hydroxybenzoic acid (HBA) as synergists of indole-3-butyric acid (IBA) in the rooting of single node stem cuttings of T. cacao, and showed both an increase in rhizogenesis and peroxidase activity in stem cuttings treated with either or both HBA and IBA as compared with controls, and showed that increased peroxidase levels
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Ashton Sean Michael Vincent
Grey Debbie
Scollick Sandra Jane
Spencer Margaret Elizabeth
Stafford Angela Marian
Marx Irene
Phytera, Inc.
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