Method of enhancing enzyme activity and enzyme solution...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S176000, C435S181000, C435S188000

Reexamination Certificate

active

07892805

ABSTRACT:
A method of enhancing the intrinsic activity of an enzyme in a raw enzyme solution, the method comprising treating the raw enzyme solution with an effective amount of a purifying agent, most preferably, activated carbon, to effect the enhancement and provide an enzyme solution of enhanced activity. Preferred enzymes are amylase, glucoamylase, cellulase, xylanase, and all other group 3 hydrolases.

REFERENCES:
patent: 4204041 (1980-05-01), Bailey et al.
patent: 6582606 (2003-06-01), Lausten et al.
patent: 2002/0020668 (2002-02-01), Lausten et al.
patent: 1 082 370 (1967-09-01), None
patent: 1091347 (1967-11-01), None
patent: 1 507 792 (1978-04-01), None
patent: 560003631 (1981-01-01), None
patent: 560003632 (1981-01-01), None
patent: 60092433 (1985-05-01), None
patent: 90071 (1986-08-01), None
Schuster et al., The effect of charcoal treatment on microsomal Cytochrome P-450, FEBS letters, vol. 74, Feb. 1977, p. 107-110.
Aikat et al, Biotechnology Letters, vol. 23, 2001, p. 295-301.
Bailey et al, Biotechnology adn Bioengineering, vol. 25, 1983, p. 1923-1935.
http://www.usm.maine.edu/˜rhodes/biochemLab/text/HdtPurLys/HDTPurLys03.html, Oct. 8, 2002.
http://www.ap-lab.com/circular—dichroism.htm, Jul. 6, 2006.
Shenoy et al , Journal of Bioscience vol. 7, Jun. 1985 p. 399-419.
“Activated Carbon,” National Organic Standards Board Technical Advisory Panel Review Compiled by OMRI for the USDA National Organic Program, Aug. 14, 2002, pp. 1-23.
Milcent, et. al., “Clarification of Lactic Acid Fermentation Broths,” Separation and Purification Technology, 22-23 (2001) pp. 393-401.
Tsun, et. al., “Recovery and Purification of Thuringiensin from the Fermentation Broth ofBacillus thruingiensis,” Bioseparation 7: pp. 309-316 (1999).
Office Action mailed Jul. 29, 2008 in corresponding European Patent Patent Application No. 04718893.3.
Liljedahl, “Evaluation of Chromatagraphic Media for Membrane Protein Purification,” MSc. Thesis, Uppsala University School of Engineering, 2001, pp. 1-20.
Kerkhoff et al., “Solubilization, Partial Purification and Photolabeling of the Integral Membrane Protein Lysophospholipid:acyl-CoA Acyltransferase (LAT),” Eur. J. Biochem, 267, 6339-6345 (2000).
Cornell lab manual for BIOBM330. http://instruct1.cit.cornell.edu/Courses/biobm330/protlab/Strategy.html, obtained from internet May 1, 2007.
Instructional materials for the MATC Biotechnology program in Madison, WI http://matcmadison.edu/biotech/resources/proteins/labManual/chapter—1.htm, obtained from internet May 1, 2007.
Wingfield et al., Purification and characterization of a methionine-specific aminopeptidase fromSalmonella typhimurium, Eur. J Biochem. 180.23-32 (1989).
MacKay et al., “Identification and Isolation of a 155-KDa Protein with Neuropathy Target Esterase Activity,” Fundamental and Applied Toxicology, vol. 30, pp. 23-30, (1996).
Pimenov et al., “The Adsorption and Deactivation of Microorganisms by Activated Carbon Fiber,” Separation Science and Technology 36(15), 3385-3394, (2001).
Hydamaka et al., “Control of Color Problems During Recycling of Food Process Waters,” Food Science Department at the University of Manitoba, pp. 237-256, Dec. 1976 Environmental Protection Technology Series v. 600/2-76-304.
Kelly, et. al., “The Use of Circular Dichroism in the Investigation of Protein Structure and Function,” Curr. Protein and Peptide Sci., 1, 349-384, (2000).
Lendenmen, et. al., “2-Aminophenol 1,6-Dioxygenase: a Novel Aromatic Ring Cleavage Enzyme Purified fromPseudomonas pseudoalcaligenesJS45,” J. Bacteriol., pp. 6227-6232, (1996).
Chen et al., “D-Ribulose-5-Phosphate 3-Epimerase: Cloning and Heterologous Expression of the Spinach Gene, and Purification and Characterization of the Recombinant Enzyme,” Plant Physiol. 118: 199-207, (1998).
Walsh, “Proteins: Biochemistry and Biotechnology,” Wiley, West Sussex, England. pp. 156-161 (2002).
Sadana, “Bioseparation of Proteins,” Academic Press, San Diego, pp. 1-15, 135, 136, 178, 187, and 245 (1998).
Ladisch, et. al., “Protein Purification: From Molecular Mechanisms to Large Scale Processes,” ACS Symposium Series 427 (1990).
Bailon, et. al., “Recovery of Recombinant Proteins by Immunoaffinity Chromatography”, pp. 150-167, 1990.
Harrison, “Protein Purification Process Engineering,” Marcel Dekker, New York, pp. 6, 7, 44, 45, 52, 53, 128-131, 136, 137, 146, 147, 152-155, 172-175, 210 and 211(1994).
Stein, “Fundamentals of Protein Biotechnology,” Marcel Dekker, New York, pp. 145, 161, and 162 (1990).
Wheelwright, “Protein Purification: Design and Scale up of Downstream Processing,” Hanser Publishers, Munich, pp. 32, 33, 62, 63, 80, 82, 172, and 186 (1991).
Davis, “Covalent immobilisation of laccase on activated carbon for phenolic effluent treatment”, Appl Microbiol Biotechnol (1992) 37:474-479.
Sotiropoulou, et. al, “Lowering the detection limit of the acetylcholinesterase biosensor using a nanoporous carbon matrix”, Analytica Chimica Acta 530 (2005) 199-204.
Kibarer, et. al., “Optimization studies on the features of an activated charcoal-supported urease system, Biomaterials”. vol. 17, No. 15, pp. 1473-1479. (1996).
Roth, et. al., β-Galactosidases (Escherichia coli) with Double Substitutions Show That Tyr-503 Acts Independently of Glu-461 but Cooperatively with Glu-537, Journal of Protein Chemistry, vol. 22, Nos. 7/8, Nov. 2003.
Majunath, et. al., “Fungal glucoamylases,” J. Appl. Biochem., vol. 5, pp. 235-260 (1983.
International Search Report for PCT/CA2004/000370, Jul. 2, 2004.
Bgibeaut, David M, “Synthesis of (1-3), (1-4)-Beta-D-Glucan in the Golgi Apparatus of Maize Ceoleoptiles,” Proceedings of the National Academy of Sciences of the U.S., vol. 90, No. 9, 1993, pp. 3850-3854.
Schuster, I, “The Effect of Charcoal Treatment on Microsomal Cytochrome P-450,” FEBS Letters, vol. 74, No. 1, 1977, pp. 107-110.
Rani, A, “Preparation and Characterization of Amyloglucosidase Adsorbed on Activated Charcoal,” Journal of Molecular Catalysis B Enzymatic, vol. 10, No. 5, Oct. 2000, pp. 471-476.
Cho, Y, “Immobilization of Enzymes on Activated Carbon Properties of Immobilized Gluco Amylase EC-3.2.1.3 Glucose Oxidase EC-1.1.3.4 and Glucono Lactonase,” Biotecnology and Bioengineering, vol. 20, No. 10, 1978, pp. 1651-1665.

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

Method of enhancing enzyme activity and enzyme solution... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method of enhancing enzyme activity and enzyme solution..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method of enhancing enzyme activity and enzyme solution... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2637332

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