The Procter Gamble Company

Genencor International, Inc.

Lori Jean Wilson

Richard Ray Bott

Thomas P Graycar

Andre Cesar Baeck

Chanchal Kumar Ghosh

Donn N Rubingh

Philip Frederick Brode, Iii

Bobby Lee Barnett

Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions +76 in combination with one or more of the following residues +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274 insubtilisin.

Subtilisin variants

Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions &plus;76 in combination with one or more of the following residues &plus;99, &plus;101, &plus;103, &plus;104, &plus;107, &plus;123, &plus;27, &plus;105, &plus;109, &plus;126, &plus;128, &plus;135, &plus;156, &plus;166, &plus;195, &plus;197, &plus;204, &plus;206, &plus;210, &plus;216, &plus;217, &plus;218, &plus;222, &plus;260, &plus;265 and/or &plus;274 in subtilisin.

Subtilisin variants multiply-substituted subtilising variants having a substitution at position 76

The present invention relates to cleaning compositions comprising protease enzyme which is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived by replacement of a plurality of amino acid residues of a precursor carbonyl hydrolase with different amino acids, wherein said plurality of amino acid residues replaced in the precursor enzyme correspond to position +76 in combination with one or more of the following residues: +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274, where the numbered positions corresponds to naturally-occurring subtilisin from Bacillus amyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins (such as Bacillus lentus subtilisin).

Protease-containing cleaning compositions

The present invention relates to cleaning compositions comprising subtilisin proteases from Bacillus lentus having the following alterations: N76D, S103A and V104I, where the numbering is based on the corresponding positions in the subtilisin from Bacillus amyloliquefaciens.

Growing community of inventors

Millbrae, CA, United States of America

Lori Jean Wilson