Mutated alkaline cellulase

Details Mutated alkaline cellulase Mutated alkaline cellulase

2008-04-29

2008-04-29

Prouty, Rebecca E (Department: 1652)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S069100, C435S091100, C435S252300, C435S320100, C435S471000, C536S023200

Reexamination Certificate

active

07364891

ABSTRACT:
A mutated alkaline cellulase derived from a cellulase having the amino acid sequence represented by SEQ ID NO: 1 or one having a homology of at least 90% therewith by deleting one or more amino acid residues from the 343- to 377-positions in SEQ ID NO: 1 or a region corresponding thereto and then inserting a peptide having from 2 to 15 amino acid residues into the deletion site; and a gene encoding the same. The above alkaline cellulase has an optimum pH value close to the pH value of laundry water and, therefore, is useful as an enzyme for detergents.

REFERENCES:
patent: 0 269 977 (1988-06-01), None
patent: 2001231569 (2001-08-01), None
Sumitomo et al., Nucleotide sequence of the gene for an alkaline endoglucanase from an alkalophilicBacillusand its expression inEscherichia coliandBacillus subtilis. Biosci. Biotech. Biochem., 1992 vol. 56 (6): 872-877.
Whisstock et al., Prediction of protein function from protein sequence and structure. Q. Rev. Biophysics., 2003. vol. 36 (3): 307-340.
Jae-Seon Park, et al., “Identification of two amino acids contributing the high enzyme activity in the alkaline pH range of an alkaline endoglucanase from aBacillussp.”, Protein Engineering, vol. 6, No. 8, XP-009048909, 1993, pp. 921-926.
Katsuya Ozaki, et al., “Molecular cloning and nucleotide sequence of a gene for alkaline cellulase fromBacillussp. KSM-635”, Journal of General Microbiology, vol. 136, XP-002225733, Jul. 1990, pp. 1327-1334.
Endo, K. et al., A novel alkaline endoglucanase from an alkaliphilicBacillusisolate: enzymatic properities, and nucletide and deduced amino acid sequences., Appl. Microbiol. Biotechnol., 2001, vol. 57, Nos. 1 to 2, pp. 109 to 116.

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