Patent References Re30602 Modified enzymes and methods for making same Combining mutations for stabilization of subtilisin 5116741 Subtilisins modified at position 225 resulting in a shift in catalytic activity Non-human carbonyl hydrolase mutants, vectors encoding same and hosts transformed with said vectors Subtilisin mutants Methods of ester hydrolysis Thermally stable serine proteases Patent #: 5246849 InventorsAssigneeApplicationNo. 661378 filed on 02/28/1991US 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 compositionExaminersPrimary: Wax, Robert A.Assistant: Walsh, Stephen Attorney, Agent or FirmForeign Patent References
International ClassesC12N 009/54C12N 009/52 C11D 007/42 C11D 003/386 Foreign Application Priority Data1989-08-31 DEAbstractNovel, 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 The result is highly alkaline proteases in which original amino acids have been replaced by more strongly basic amino acids, preferably by the amino acids lysine or arginine.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
|
| ||||||||||||||