Glucose isomerases with an altered pH optimum

Details Glucose isomerases with an altered pH optimum Glucose isomerases with an altered pH optimum

1993-08-26

1995-01-24

Wax, Robert A.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Isomerase

435 691, 4351723, 435252, 435 3257.33, 536 232, 935 10, 935 14, 935 60, 935 72, 935 75, C12N 1361, C12N 992, C12N 1570, C12N 1574

Patent

active

053842570

ABSTRACT:
A method for selecting amino acid residues is disclosed which upon replacement will give rise to an enzyme with an altered pH optimum. The method is specific for metalloenzymes which are inactivated at low pH due to the dissociation of the metal ions. The method is based on altering the pK.sub.a of the metal coordinating ligands or altering the K.sub.ass for the metal binding. New glucose isomerases with an altered pH optimum are provided according to this method. These altered properties enable starch degradation to be performed at lower pH values.

REFERENCES:
patent: 4609625 (1986-09-01), Keyes et al.
patent: 4894331 (1990-06-01), Ratzkin et al.
patent: 5041378 (1991-08-01), Drummond et al.
Collyer, C. A., et al., Mar. 1990, Journal of Molecular Biology, 212(1): 211-235.
Henrik, K., et al., 1989, Journal of Molecular Biology, 208(1): 129-157.
Batt, C. A., et al., Jan. 1990, Proceedings of the National Academy of Sciences, U.S.A., 87: 618-622.
Carrell, H. L., et al., 1989, Proceedings of the National Academy of Sciences, U.S.A., 86: 4440-4444.
Amore, R., et al., 1989, Nucleic Acids Research, 17(18): 7515.
Procourt, P., et al., 1988 Nucleic Acids Research, 16(19): 9337.
Muraki, M., et al., 1988, Protein Engineering, 2(1): 49-54.
Zvelebil, M. J. J. M., et al., 1988, Protein Engineering, 2(2): 127-138.
Farber, G. K., et al., 1988, Proceedings of the National Academy of Sciences, U.S.A., 85: 112-115.
Farber, G. K., et al., 1987, Protein Engineering, 1:467-469.
Henrik, K., et al., 1987, Protein Engineering, 1: 459-460.
Saari, G. C., et al., 1987, Journal of Bacteriology, 169(2): 612-618.
Sternberg, M. J. E., et al., 1987, Nature, 330: 86-88.
Wells, J. A., et al., 1987, Proceedings of the National Academy of Sciences, U.S.A., 84: 1219-1223.
Russel, A. J., et al., 1987, Journal of Molecular Biology 193: 803-813.
Thomas, P. G., et al., 1987, Nature, 318: 375-376.
Chen, "Glucose Isomerase (a Review)", Process Biochemistry, pp. 30-35 (Jun./Jul. 1980).
Chen, "Glucose Isomerase (a Review)", Process Biochemistry, pp. 36-41 (Aug./Sep. 1980).
Farber et al., "the 3.0 .ANG. crystal structure of xylose isomerase from Streptomyces olivochromogenes", Protein Eng. 1:459-466 (1987).
Rey et al., "Structure Analysis of the 2.8 .ANG. Model of Xylose Isomerase From Actinoplanes missouriensis", Proteins 4:165-172 (1987).
Henrick et al., "Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter", Protein Eng. 1:467-475 (1987).
Callens et al., "D-Xylose isomerase from Streptomyces violaceoruber: structural and catalytic roles of bivalent metal ions", Enzyme Microb. Technol. 10:695-700 (1988).
R. van Tilbert, Thesis entitled "Engineering Aspects of Biocatalysts in Industrial Starch Conversion Technology", Delftse Universitaire Pers (1983).

Affiliated with

Also associated with

Rating

Glucose isomerases with an altered pH optimum does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Glucose isomerases with an altered pH optimum, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Glucose isomerases with an altered pH optimum will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-1468259