Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing compound containing saccharide radical
Patent
1990-06-29
1992-11-10
Wax, Robert A.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing compound containing saccharide radical
435205, 435201, 4351723, 435 691, C12P 1920, C12N 934, C12N 926, C12N 1500
Patent
active
051622106
ABSTRACT:
A process for converting starch or partially hydrolyzed starch into a syrup containing dextrose includes the steps of saccharifying starch hydrolyzate in the presence of a saccharifying starch hydrolyzate in the presence of a mutated glucoamylase or related enzyme and increasing the selectivity of the enzyme for .alpha.-(1.fwdarw.4)-glucosidic bonds by the glucoamylase or related enzyme by including at least one mutation, the mutation substituting an amino acid of the enzyme with at least one amino acid chosen by comparison with structurally related regions of other enzymes that selectively hydrolyze only .alpha.-(1.fwdarw.4) glucosidic bonds.
Enzymes made in accordance with the present invention are also disclosed.
REFERENCES:
patent: 4560651 (1985-12-01), Nielsen et al.
Svensson, B., et al., 1983, Carlsberg Research Communications 48:529-544.
Svensson, B., et al., 1986, European Journal of Biochemistry 154:497-502.
Hakansson, K., et al., 1989, Carlsberg Research Communications 54:145-156.
Svensson, B., et al., 1990, European Journal of Biochemistry 188:29-38.
Meagher, M. M., et al., 1989, Biotechnology and Bioengineering, vol. 34, No. 5:689-693.
Leatherbarrow, R. J., et al., 1986, Protein Engineering, vol. 1, No. 1: 7-16.
Harada, T., 1984, Biotechnology and Genetic Engineering Reviews, vol. 1: 39-63.
Tanaka, Y. et al., (1986) Comparison of amino acid sequence of three glucoamylases and their structure function relationships, Agric. Biol. Chem., 50, 965-969.
Itoh T., et al., (1987) Nucleotide sequence of the glucoamylase gene GLU1 in yeast Saccaromycopsis fibuligera. J. Bacteriol., 169, 4171-4176.
Hiromi, K., (1970) Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions, Evaluation of subsite affinities of exo-enzyme, biochem. Biophys. Res. Commun., 40, 1-6.
Savek'ev, A. N. et al., (1982) Carboxyl groups in active site of glucoamylase from Aspergillus awamori, Biochemistry (USSR), 47, 1365-1367.
Tanaka, A. et al., (1983) Fractionation of Isozymes and determination of the subsite structure of glucoamylase form Rhizopus niveus. Agr. Biol. Chem., 47, 573-580.
Koyama, T., et al., (1984) subsite affinity of the glucoamylase from Aspergillus saitoi. Chem. Pharm. Bull., 32, 757-761.
Meagher, M. M., (1989) Subsite mapping of Aspergillus niger Glucoamylases I and II with malto-and isomaltooligosaccharides, Biotechnol. Bioeng., 34, 681-688.
Svensson, B. (1988) Regional distant sequence homology between amylases, a-glucosidases and transglucanosylases, FEBS Lett., 230, 72-76.
Nikolov, Z. L., et al., (1989) Kinetics, equilibria and modeling of the formation of oligosaccharides from D-glucose with Aspergillus niger glucoamylases I and II, Biotechnol. Bioeng., 34, 694-704.
Sierks, M. R. et al., (1989) Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori glucoamylase, Protein Eng., 2, 621-625.
Sierks, M. R., et al.,(1990) Catalytic Mechanism of fungal (Glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Asperigillus awamori, Protein Eng., 3, 193-198.
Pazur, J. H. et al., (1967) Properties of the glucoamylase from Rhizopus delemar, Carbohydr. Res., 4, 371-379.
Watanabe, T. et al., (1969) Reversion product from D-glucose by purified Phizopus niveus glucoamylase, Starke, 21, 18-21.
Watanabe, T. et al., (1969) Reversion product from D-glucose by purified Endomyces sp. glucoamylase. Starke, 21, 44-47.
Hehre, E. J. et al., (1969) Configurational specificity unappreciated key to understanding enzymic revrsions and de novo glucosidic bond synthesis. Arch. Biochem. Biophys., 135, 75-89.
Pazur, J. H. et al., (1977) Comparison of the action of glucoamylase and glucoslytransferase on D-glucose, maltose, and malto-oligosaccharides. Carbohydr. Res., 58, 193-202.
Pazur, J. H. et al., (1959) The action of an amyloglucosidase of Aspergillus niger on starch and maltooligodextrins. J. Biol. Chem., 234, 1966-1970.
Clarke, A. J. & Svensson, B. (1984) Identification of an essential tryptophonyul residue in the primary structure of glucoamylase G2 from Aspergillus niger. Carlsberg Res. Comman., 49, 559-566.
Innis, M. A. et al., (1985) Expression, Glycoslyation, and secretion of an Aspergillus glucoamylase by Saccaromyces cerevisiae, Science, 228, 21-26.
Sierkes, M. R., (1988) Ph. D. Thesis, Iowa State University.
Bock, K & Sigursshojold, B. W. (1989) Mechanism and binding specificity of B-glucosidase catalyzed nydrolysis of cellobiase analogues studied by competition enzyme kinetics monitored by HNMR spectroscopy Eur. J. Biochem., 178, 711-720.
Sierks Michael
Svensson Birte
Iowa State University Research Foundation
Moore William W.
Wax Robert A.
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