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Highly alkaline proteases

Patent 5352603 Issued on October 4, 1994. Estimated Expiration Date: Icon_subject October 4, 2011. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.

Patent References

Re30602

Modified enzymes and methods for making same
Patent #: 4760025
Issued on: 07/26/1988
Inventor: Estell ,   et al.

Combining mutations for stabilization of subtilisin
Patent #: 4990452
Issued on: 02/05/1991
Inventor: Bryan, et al.

5116741

Subtilisins modified at position 225 resulting in a shift in catalytic activity
Patent #: 5155033
Issued on: 10/13/1992
Inventor: Estell, et al.

Non-human carbonyl hydrolase mutants, vectors encoding same and hosts transformed with said vectors
Patent #: 5182204
Issued on: 01/26/1993
Inventor: Estell, et al.

Subtilisin mutants
Patent #: 5185258
Issued on: 02/09/1993
Inventor: Caldwell, et al.

Methods of ester hydrolysis
Patent #: 5244791
Issued on: 09/14/1993
Inventor: Estell

Thermally stable serine proteases Patent #: 5246849
Issued on: 09/21/1993
Inventor: Bryan, et al.

Inventors

Assignee

Application

No. 661378 filed on 02/28/1991

US Classes:

435/221, Bacteria is bacillus435/212, Acting on peptide bond (e.g., thromboplastin, leucine amino-peptidase, etc., (3.4))435/219, Proteinase510/306, Proteolytic enzyme510/320, Enzyme component of specific activity or source (e.g., protease, of bacterial origin, etc.)510/321, Liquid composition (e.g., slurry, etc.)510/392, Enzyme component of specific activity or source (e.g., protease, of bacterial origin, etc.)510/393, Liquid composition (e.g., slurry, etc.)510/530Enzyme composition

Examiners

Primary: Wax, Robert A.
Assistant: Walsh, Stephen

Attorney, Agent or Firm

Foreign Patent References

  • 130756 EP. 12/22/1984
  • 328229 EP. 08/22/1989
  • 0405901A1 EP. 01/22/1991
  • 0405902A1 EP. 01/22/1991
  • WO91/00345 WO. 01/22/1991
  • 8906279 WO. 07/22/1989

International Classes

C12N 009/54
C12N 009/52
C11D 007/42
C11D 003/386

Foreign Application Priority Data

1989-08-31 DE

Abstract

Novel, optimized highly alkaline proteases which are suitable for use in detergent formulations are prepared by employing microorganisms transformed by mutated DNA sequences. The mutated sequences are obtained starting from DNA sequences which code for highly alkaline protease usually produced by Bacillus species by altering these DNA sequences in defined positions by directed mutagenesis (point mutation) in such a way that the codon in which the point mutation is located now codes for an amino acid which is more strongly basic than the original amino acid. The result is highly alkaline proteases in which original amino acids have been replaced by more strongly basic amino acids, preferably by the amino acids lysine or arginine. Synthetic oligonucleotides, DNA sequences, vectors and transformed microorganisms which are used for generating and obtaining the optimized highly alkaline protease are also described.

Other References

  • Meloun et la, FEBS Letters 183:195-199, Apr. 1985
  • Reeck et al., "Homology' in Proteins and Nucleic Acids . . . ", Cell 50: 667, Aug. 28, 1987
  • Dayhoff, Atlas of Protein Sequence and Structure, 1972 p. 96
  • Creighton, Proteins, 1983, p. 7
  • Shulz and Schirmer, Principles of Protein Structure, 1979, pp. 14-16
  • Wells et al., "Subtilisin-an enzyme designed to be engineered", Trends in Biochemical Sciences, 13:291-97 (1988
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