Abstract: The invention includes novel fusion nucleic acids encoding fusion polypeptides which when expressed in a filamentous fungus result in the expression of fusion polypeptides. The fusion nucleic acids comprise four nucleic acids which encode a fusion polypeptide comprising first, second, third and fourth amino acid sequences. The first nucleic acid encodes a signal polypeptide functional as a secretory sequence in a first filamentous fungus. The second nucleic acid encodes a secreted polypeptide or functional portion thereof which is normally secreted from the same filamentous fungus or a second filamentous fungus. The third nucleic acid encodes a cleavable linker while the fourth nucleic acid comprises at least two nucleic acids encoding desired polypeptides.

Abstract: A mutant cellulase obtainable from Thermomonospora spp is provided which differs from a precursor cellulase in that it has been genetically engineered to introduce a substitution, deletion or addition of an amino acid residue to said precursor cellulase which provided improved activity in a detergent. Preferably, the substitution is at a residue corresponding to T140 in Thermomonospora fusca.

Abstract: Novel alpha-amylase mutants derived from the DNA sequences of naturally occurring or recombinant alpha-amylases are disclosed. The mutant alpha-amylases, in general, are obtained by in vitro modifications of a precursor DNA sequence encoding the naturally occurring or recombinant alpha-amylase to generate the substitution (replacement) or deletion of one or more oxidizable amino acid residues in the amino acid sequence of a precursor alpha-amylase. Such mutant alpha-amylases have altered oxidative stability and/or altered pH performance profiles and/or altered thermal stability as compared to the precursor. Also disclosed are detergent and starch liquefaction compositions comprising the mutant amylases, as well as methods of using the mutant amylases.

Abstract: Novel alpha-amylase mutants derived from the DNA sequences of naturally occurring or recombinant alpha-amylases are disclosed. The mutant alpha-amylases, in general, are obtained by in vitro modifications of a precursor DNA sequence encoding the naturally occurring or recombinant alpha-amylase to generate the substitution (replacement) or deletion of one or more oxidizable amino acid residues in the amino acid sequence of a precursor alpha-amylase. Such mutant alpha-amylases have altered oxidative stability and/or altered pH performance profiles and/or altered thermal stability as compared to the precursor. Also disclosed are detergent and starch liquefaction compositions comprising the mutant amylases, as well as methods of using the mutant amylases.

Abstract: There are described processes for expressing a lipase in a heterologous host. Further described are transformed cells comprising heterologous DNA and particular plasmids containing heterologous fusion DNA constructs.

Abstract: Processes for producing various heterologous polypeptides which when expressed are either incorrectly processed and hence asssociated with the surface of the host cell or are not processed to mature form. More specifically, processes for the production of heterologous non-human carbonyl hydrolases expressed either in host cells incapable of producing enzymatically active endoprotease or host cells deficient in enzymatically active extracellular endoprotease are disclosed. Such non-human carbonyl hydrolases generally are incapable of autoproteolytic maturation and become associated with the surface of expression hosts which are deficient in enzymatically active extracellular endoprotease. Processes for preparing non-human carbonyl hydrolase and heterologous polypeptides which are expressed as part of a fusion polypeptide are also disclosed, as well as non-human carbonyl hydrolases which are substantially free of the host cell membrane with which they are normally associated.

Abstract: A substantially enzymatically pure hydrolase is provided which is secreted by and isolatable from Pseudomonas mendocina ATCC 53552. Cloning the gene expressing the hydrolase into a suitable expression vector and culturing, such as fermenting the E. coli strain JM101 harboring a plasmid designated pSNtacII, has been found to provide surprisingly high yields of the hydrolase.

Abstract: Novel carbonyl hydrolase mutants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases. The mutant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to encode the substitution of an amino acid in the amino acid sequence of a precursor carbonyl hydrolase. Such mutants have properties which are different than the precursor hydrolase.

Abstract: An enzymatic perhydrolysis system, useful for bleaching, has a novel enzyme, a substrate, and a source of hydrogen peroxide, and provides in situ formation of peracid in aqueous solution. The substrate is selected for enzyme catalyzed reaction, and preferably is an acylglycerol with two or three fatty acid chains. The enzyme is hydrolytically and perhydrolytically active even in the presence of anionic surfactants, has lipase activity, and is isolatable from Pseudomonas putida ATCC 53552.