Use of thiol redox proteins for reducing protein intramolecular

Food or edible material: processes – compositions – and products – Fermentation processes – Of farinaceous cereal or cereal material

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

426 19, 426 23, 426 27, 426 94, 426549, 426557, 426618, 426622, 426496, 426451, 530374, 530375, 435 691, 435189, 4352551, A21D 1000, A21D 1306, A21D 226, A23J 314, C07K 14415, C12P 2106, C12N 902, C12N 119

Patent

active

061139513

DESCRIPTION:

BRIEF SUMMARY
FIELD OF THE INVENTION

The present invention relates to the use of thiol redox proteins to reduce seed protein such as cereal proteins, enzyme inhibitor proteins, venom toxin proteins and the intramolecular disulfide bonds of certain other proteins. More particularly, the invention involves use of thioredoxin and glutaredoxin to reduce gliadins, glutenins, albumins and globulins to improve the characteristics of dough and baked goods and create new doughs and to reduce cystine containing proteins such as amylase and trypsin inhibitors so as to improve the quality of feed and cereal products. Additionally, the invention involves the isolation of a novel protein that inhibits pullulanase and the reduction of that novel protein by thiol redox proteins. The invention further involves the reduction by thioredoxin of 2S albumin proteins characteristic of oil-storing seeds. Also, in particularly the invention involves the use of reduced thiol redox agents to inactivate snake neurotoxins and certain insect and scorpion venom toxins in vitro and to treat the corresponding toxicities in individuals.
This invention was made with government support under Grant Contract Nos. DCB 8825980 and DMB 88-15980 awarded by the National Science Foundation. The United States Government has certain rights in this invention.


BACKGROUND OF THE INVENTION

Chloroplasts contain a ferredoxin/thioredoxin system comprised of ferredoxin, ferredoxin-thioredoxin reductase and thioredoxins f and m that links light to the regulation of enzymes of photosynthesis (Buchanan, B. B. (1991) "Regulation of CO.sub.2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Perspective on its discovery, present status and future development", Arch. Biochem. Biophys. 288:1-9; Scheibe, R. (1991), "Redox-modulation of chloroplast enzymes. A common principle for individual control", Plant Physiol. 96::1-3). Several studies have shown that plants also contain a system, analogous to the one established for animals and most microorganisms, in which thioredoxin (h-type) is reduced by NADPH and the enzyme, NADP-thioredoxin reductase (NTR) according to the following: ##STR1## (Florencio F. J., et al. (1988), Arch. Biochem. Biophys. 266:496-507; Johnson, T. C., et al. (1987), Plant Physiol. 85:446-451; Suske, G., et al. (1979), Z. Naturforsch. C. 34:214-221). Current evidence suggests that the NADP/thioredoxin system is widely distributed in plant tissues and is housed in the mitochondria, endoplasmic reticulum and cytosol (Bodenstein-Lang, J., et al. (1989), FEBS Lett. 258:22-26; Marcus, F., et al. (1991), Arch. Biochem. Biophys. 287:195-198).
Thioredoxin h is also known to reductively activate cytosolic enzyme of carbohydrate metabolism, pyrophosphate fructose-6-P, 1-phosphotransferase or PFP (Kiss, F., et al. (1991), Arch. Biochem. Biophys. 287:337-340).
The seed is the only tissue for which the NADP/thioredoxin system has been ascribed physiological activity in plants. Also, thioredoxin h has been shown to reduce thionins in the laboratory (Johnson, T. C., et al. (1987), Plant Physiol. 85:446-451). Thionins are soluble cereal seed proteins, rich in cystine. In the Johnson, et al. investigation, wheat purothionin was experimentally reduced by NADPH via NADP-thioredoxin reductase (NTR) and thioredoxin h according to Eqs. 2 and 3. ##STR2##
Cereal seeds such as wheat, rye, barley, corn, millet, sorghum and rice contain four major seed protein groups. These four groups are the albumins, globulins, gliadins and the glutenins or corresponding proteins. The thionins belong to the albumin group or faction. Presently, wheat and rye are the only two cereals from which gluten or dough has been formed. Gluten is a tenacious elastic and rubbery protein complex that gives cohesiveness to dough. Gluten is composed mostly of the gliadin and glutenin proteins. It is formed when rye or wheat dough is washed with water. It is the gluten that gives bread dough its elastic type quality. Flour from other major crop cereals barley, corn, sorghum, oat, millet and

REFERENCES:
patent: 3803326 (1974-04-01), Craig et al.
patent: 4405648 (1983-09-01), Atsumi et al.
patent: 5028419 (1991-07-01), Pigiet
Blomback et al. Enzymic reduction of disulfide bonds in fibrinogen by the thioredoxin system. I Identification of reduced bonds and studies on reoxidation process. Thrombosis Research. 4 (1) 55-75 1974.
Holmgren et al. Enzymic reduction of disulfide bonds by thioredoxin. The reactivity of disulfide bonds in human choriogonadotropin and its subunits. European J. Biocehemistry 70(2):377-83 1976.
Muller et al. Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J. Biological Chemistry 266 (14): 9194-9202 May 15, 1991.
Rothenbuhler et al., "Disulfide Reduction and Molecular Dissociation Improves the Proteolysis of Soy Glycinin by Pancreatin in vitro," Journal of Food Science, 51(6):1479-1482, (1986).
Astwood et al., "Stability of Food Allergens to Digestion in Vitro," Nature Biotechnology, 14(10): 1269-1273, (1996).
Buchanan et al., "Thioredoxin-linked Mitigation of Allergic Responses to Wheat," Proceedings of the National Academy of Sciences of the United States of America, 94(10): 5372-5377 (1997).
Buchanan et al., "Thioredoxin: A Multifunctional Regulatory Protein with a Bright Future in Technology and Medicine," Archives of Biochemistry and Biophysics, 314(2): 257-260, (1994).
Holmgren (1979), "Reduction of disulfides by thioredoxins," J. Biol. Chem 254:9113-9119.
Holmgren (1985), "Thioredoxin," Ann. Rev. Biochem. 54:237-271.
Droux, M. et al. (1987) "Ferredoxin-Thioredoxin Reductase, an Iron-Sulfur Enzyme Linking Light to Enzyme Regulation in Oxygenic Photosynthesis: Purification and Properties of the Enzyme from C.sub.3, C.sub.4, and Cyanobacterial Species", Archives of Biochemistry and Biophysics 252(2):426-439.
Marcus, F. et al. (1988) "Comparative amino acid sequence of fructose-1,6-bisphosphatases: Identification of a region unique to the light-regulated chloroplast enzyme", Proc. Natl. Acad. Sci. USA 85:5379-5383.
Raines, C.A. et al. (1988) "Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene", Nucleic Acids Research 16:7931-7942.
Decottignies, P. et al. (1988) "Primary Structure of the Light-dependent Regulatory Site of Corn NADP-Malate Dehydrogenase", The Journal of Biological Chemistry 263(24):11780-11785.
Miki, J. et al. (1988) "The .gamma.-subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence" FEBS 232(1):221-226.
Porter, M.A., et al. (1988) "Characterization of the Regulatory Thioredoxin Site of Phosphoribulokinse", The Journal of Biological Chemistry 263(1):123-129.
Schiavo, G. et al. (1990) "An Intact Interchain Disulfide Bond Is Required for the Neurotoxicity of Tetanus Toxin", Infection and Immunity 58(12):4136-4141.
Muller, R.G.D. "Thioredoxin Deficiency In Yeast Prolongs S Phase and Shortens the G1 Interval of the Cell Cycle," The Journal of Biological Chemistry 266:9194-9202 (1991).
Dahle et al., "The Weakening Action of Thioctic Acid in Unyeasted and Yeasted Doughs," Cereal Chem., 43:682-688 (1966).
Florencio et al., "An NADP/Thioredoxin System in Leaves: Purification and Characterization of NADP-Thioredoxin Reductase and Thioredoxin ih from Spinach," Arch. Biochem. Biophys., 266(2):496-507 (1988).
Crawford et al., "Evidence for Function of the Ferredoxin/Thioredoxin System in the Reductive Activation of Target Enzymes of Isolated Intact Chloroplasts," 27(1):223-239 (1989).
Yamada, "Inactive Debranching-Enzyme in Rice Seeds, and its Activation," Carbohydrate Research, 90:253-157 (1981).
Wada et al., "Purothionin: A Seed Protein with Thioredoxin Activity," FEBS Letters, 124(2):237-240 (1981).
Russel et al, "Sequence of Thioredoxin Reductase from Escherichia coli," J. Biol. Chem., 263(18):9015-9019 (1988).
Holmgren et al., "Thioredoxin and Glutaredoxin Systems" J. Biol. Chem., 264(24):13963-13966 (1989).
Edman et al., "Sequence of Protein Disulphide Isomerase and Implications of its Relations

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Use of thiol redox proteins for reducing protein intramolecular does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Use of thiol redox proteins for reducing protein intramolecular , we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Use of thiol redox proteins for reducing protein intramolecular will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2209501

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.