Amylolytic enzymes derived from the B.licheniformis...

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

Reexamination Certificate

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C424S093300, C424S093460, C424S246100, C435S022000, C435S099000, C435S201000, C435S202000, C435S221000, C435S222000, C435S252310, C435S252200, C536S023700

Reexamination Certificate

active

06939703

ABSTRACT:
The present invention relates to novel amylolytic enzymes having improved characteristics for the use in starch degradation, in textile or paper desizing and in household detergent compositions. The disclosed α-amylases show surprisingly improved properties with respect to the activity level and the combination of thermostability and a higher activity level. These improved properties make them more suitable for the use under more acidic or more alkaline conditions. The improved properties allow also the reduction of the Calcium concentration under application conditions without a loss of performance of the enzyme.

REFERENCES:
patent: PCT/DK 93/00230 (1993-07-01), None
patent: 0414297 (1996-10-01), None
patent: 2676456 (1991-05-01), None
patent: WO 91/00353 (1991-01-01), None
patent: WO 94/02597 (1994-02-01), None
patent: WO 94/18314 (1994-08-01), None
Brady et al., “Solution of the Structure ofAspergillus nigerAcid α-Amylase by Combined Molecular Replacement and Multiple Isomorphous Replacement Methods,”Acta Cryst(1991) B47:527-535.
Ho et al., Site-directed mutagenesis by overlap extension using the polymerase chain reaction,Gene(1989) 77, pp. 51-59.
Holm et al., “Random mutagenesis used to probe the structure and function ofBacillus stearothermophilusalpha-amylase,”Prot. Engineering(1990) 3:181-191.
Nagashima et al., “Site-directed Mutagenesis of Catalytic Active-site Residues of Taka-amylase A”,Biosci. Biotech. Biochem.,56(2). 207-210, 1992.
Qian et al., “Structure and Molecular Model Refinement of Pig Pancreatic α-Amylase at 2-1 Å Resolution,”J Mol Biol(1993) 231:785-799.
Sogaard et al., “Site-directed Mutagenesis of Histidine 93, Aspartic Acid 180, Glutamic Acid 205, Hisitidine 290, and Aspartic Acid 291 at the Active Site and Tryptophan 279 at the Raw Starch Binding Site in Barley α-amylase 1,”J Biol Chem(1993) 268:22480-22484.
Stanssens et al., “Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers”,Nucl. Acids Res.17(12) (1989) pp. 4441-4454.
Swift et al., “Structure and Molecular Model Refinement ofAspergillus oryzae(TAKA) α-Amylase: an Application of the Simulated-Annealing Method,”Acta Cryst(1991) B47:535-544.
Takase, K., “Effect of mutation of an amino acid residue near the catalytic site on the activity ofBacillus stearothermophilusα-amylase”,Eur. J. Biochem.,211 (1993) 899-902.
Vihinen et al., “Site-Directed Mutagenesis of a Thermostable α-Amylase fromBacillus stearothermophilus: Putative Role of Three Conserved Residues,”J Biochem(1990) 107:267-272.

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