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.

Oxidatively stable alpha-amylase

Depolymerization of cellulose to glucose requires the synergistic action of three key cellulases, endoglucanase (E.C. 3.2.1.4), exoglucanase (E.C. 3.2.1.176) (E.C. 3.2.1.91) and β-glucosidase (E.C. 3.2.1.21). They belong to the glycoside hydrolase (GH) family and catalyze the hydrolysis of glyosidic linkages depolymerizing cellulose to fermentable sugars. Cellulases are naturally produced by a wide spectrum of bacteria and fungi. These enzymes usually exist as cellulosomes attached to the cell wall of bacteria but are secreted into environments in fungi. They exist either as monomers or multimers with each monomer having a simple architecture containing a cellulose binding domain (CBD) and a catalytic domain (CD) interlinked by a linker peptide. Thermophilic, mesophilic and psychrophilic cellulases are quite different in their structures and amino acid compositions. Post-translational modifications such as glycosylation contribute to enzyme function, multiplicity and stability. Recent advances in recombinant DNA technology allow fast identification of novel cellulase genes, large scale production of cellulases and their genetic modifications to make tailor-made enzymes for various applications. Cellulases have been traditionally used in food processing and textile industries. The rapid depletion of fossil fuels and production of cheap fermentable sugars from abundant renewable resources have increased the demand for cellulases in lignocellulose-based biorefinery. However, the lack of a better understanding of the mechanisms of individual cellulases, their synergistic actions and their high prices are the major bottlenecks yet to be overcome for large scale commercial applications of cellulases in lignocellulose-based biorefinery.

Microbial cellulases: Engineering, production and applications

A polymer obtained through copolymerization of a monomer having a hexafluoroalcohol pendant whose hydroxyl moiety has been protected and a monomer having an acid labile group is useful as an additive to a photoresist composition for immersion lithography. When processed by immersion lithography, the resist composition exhibits good water repellency and water slip and produces few development defects.

Polymer, resist composition and patterning process

An α-amylase characterized by having a specific activity at least 25 % higher than the specific activity of Termamyl® at a temperature in the range of 25 °C to 55 °C and at a pH value in the range of pH 8 to pH 10.

Alkaline bacillus amylase

Enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved autoproteolytic stability in comparison to their wild type parent enzymes.

Subtilase variants and compositions

Included are liquid detergent compositions comprising anionic and/or nonionic surfactant, proteolytic enzyme, second enzyme, and an aromatic borate ester.

Liquid detergents with aromatic borate ester to inhibit proteolytic enzyme

Included are liquid detergent compositions containing alphahydroxyacid builder, anionic and/or nonionic surfactant, pro-teolytic enzyme, second enzyme, and a mixture of certain vicinal polyols and boric acid or its derivative The equilibrium constants for the boric/polyol reaction are K1 between about 0,1 and 400 l/mole and K2 between 0 and about 1000 l2/mole2.

Built Liquid Detergents with Boric-Polyol Complex to Inhibit Proteolytic Enzyme

Alkoxylated cationic surfactants, and mixtures thereof, are used in detergent compositions.

Alkoxylated cationic detergency ingredients

Dye transfer inhibiting compositions are disclosed, comprising: (A) a metallo catalyst selected from (a) metallo porphin and water-soluble or water-dispersible derivatives thereof; (b) metallo porphyrin and water-soluble or water-dispersible derviatives thereof; (c) metallo phthalocyanine and water-soluble or water-dispersible derivatives thereof; (B) an enzyme oxidation scavenger, (C) an enzymatic system capable of generating hydrogen peroxide, and (D) an enzyme, preferably selected from protease, lipase, amylase, and cellulase. The enzyme oxidation scavenger (B) operates to stabilize and protect the enzymes (D) from loss of activity in the wash.

Detergent compositions inhibiting dye transfer in washing

The present invention relates to dye transfer inhibiting compositions comprising: a) a polymer selected from polyamine N-oxide containing polymers which contain units having the structure formula (I), wherein P is a polymerizable unit, whereto the N--O group can be attached to or wherein the N--O group forms part of the polymerizable unit or a combination of both; A is (a), (b), (c), --O--, --S--, (d); x is =0 or 1; R are aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic groups or any combination thereof whereto the nitrogen of the N--O group can be attached or wherein the nitrogen of the N--O group form part of these groups; b) a surfactant system comprising a surfactant selected from nonionic and/or anionic and/or cationic and/or ampholytic and/or zwitterionic and/or semi-polar surfactants.

Christiaan Arthur Jacques Kamiel Thoen

Papers

Liquid detergents with aromatic borate ester to inhibit proteolytic enzyme

Built Liquid Detergents with Boric-Polyol Complex to Inhibit Proteolytic Enzyme

Alkoxylated cationic detergency ingredients

Detergent compositions inhibiting dye transfer in washing

Surfactant-containing dye transfer inhibiting compositions