Abstract: The invention is related to a non-toxic, non-toxigenic, non-pathogenic recombinant Fusarium, e.g., Fusarium graminearum host cell comprising a nucleic acid sequence encoding a heterologous protein operably linked to a promoter. The invention further relates to a method for the production of recombinant proteins using such Fusarium host cells. The invention also relates to a promoter and terminator sequence which may be used in such cells.

Abstract: A variant of a parent .alpha.-amylase enzyme having an improved washing and/or dishwashing performance as compared to the parent enzyme, wherein one or more amino acid residues of the parent enzyme have been replaced by a different amino acid residue and/or wherein one or more amino acid residues of the parent .alpha.-amylase have been deleted and/or wherein one or more amino acid residues have been added to the parent .alpha.-amylase enzyme, provided that the variant is different from one in which the methionine residue in position 197 of a parent B. licheniformis .alpha.-amylase has been replaced by alanine or threonine, as the only modification being made. The variant may be used for washing and dishwashing.

Abstract: An .alpha.-amylase characterized by having a specific activity at least 25% higher than the specific activity of Termamyl.RTM. at a temperature in the range of 25.degree. C. to 55.degree. C. and a pH value in the range of pH 8 to pH 10.

Abstract: The present invention relates to a novel metalloprotease obtainable from a fungus having increased proteolytic activity. Additionally, the invention related to isolated nucleic acid fragments encoding said metalloprotease as well as vectors, DNA constructs, and recombinant host cells comprising said nucleic acid fragments.

Abstract: A variant of a parent .alpha.-amylase enzyme having an improved washing and/or dishwashing performance as compared to the parent enzyme, wherein one or more amino acid residues of the parent enzyme have been replaced by a different amino acid residue and/or wherein one or more amino acid residues of the parent .alpha.-amylase have been deleted and/or wherein one or more amino acid residues have been added to the parent .alpha.-amylase enzyme, provided that the variant is different from one in which the methionine residue in position 197 of a parent B. licheniformis .alpha.-amylase has been replaced by alanine or threonine, as the only modification being made. The variant may be used for washing and dishwashing.

Abstract: The present invention relates to methods for obtaining a fungal host cell comprising a nucleic acid sequence encoding a heterologous polypeptide, wherein at least one cryptic splice site is modified in the nucleic acid sequence. The present invention also relates to a nucleic acid sequence(s) with a modified cryptic splice site(s) as well as nucleic acid constructs, vectors, and host cells comprising said nucleic acid sequence(s). The present invention further relates to methods for recombinant production of a polypeptide encoded by said nucleic acid sequence.

Abstract: The present invention relates to a process for providing a bleached look in the color density of the surface of dyed fabric, especially cellulosic fabric such as denim, comprising use of a phenol oxidizing enzyme such as a peroxidase or a laccase, a hydrogen peroxide source and an enhancing agent represented by formula (I).

Abstract: A variant of a parent .alpha.-amylase enzyme having an improved washing and/or dishwashing performance as compared to the parent enzyme, wherein one or more amino acid residues of the parent enzyme have been replaced by a different amino acid residue and/or wherein one or more amino acid residues of the parent .alpha.-amylase have been deleted and/or wherein one or more amino acid residues have been added to the parent .alpha.-amylase enzyme, provided that the variant is different from one in which the methionine residue in position 197 of a parent B. licheniformis .alpha.-amylase has been replaced by alanine or threonine, as the only modification being made. The variant may be used for washing and dishwashing.

Abstract: The present invention provides novel uses of compounds of general formula I: ##STR1## wherein R.sup.1, R.sup.4 and R.sup.5 are individually hydrogen, hydroxy, halogen, trifluoromethyl, lower alkyl, lower alkoxy or (tertiary amino)(lower alkoxy); and R.sup.2 and R.sup.3 are individually hydrogen or lower alkyl, or as a pharmaceutically acceptable salt thereof in combination with a pharmaceutically acceptable carrier for the manufacture of a pharmaceutical composition for the treatment or prophylaxis of atrophy of skin and/or mucous membranes.

Abstract: A glucose oxidase obtained from a Cladosporium oxysporum strain, designated as CBS 163.94, characterized by a pH-optimum in he range pH 6-7, having more than 75% of maximum activity at pH 8, determined at 30.degree. C. with D-glucose as substrate.

Abstract: The present invention relates to lipase and .alpha.-amylase variants, stabilized towards the inactiviation caused by peroxidase systems, in which variants a naturally occurring tryosine residue has been deleted, substituted with a different amino acid residue at one or more positions. The invention also relates to a method of stabilizing a lipase or an .alpha.-amylase towards the inactivation caused by the preoxidase systems, and detergent compositions comprising a lipase and/or .alpha.-amylase variant of the invention.

Abstract: A pharmaceutical formulation comprising a growth hormone and Leu-His-Leu as additive or buffering substance shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Abstract: The present invention relates to a novel metalloprotease obtainable from a fungus having increased proteolytic activity. Additionally, the invention related to isolated nucleic acid fragments encoding said metalloprotease as well as vectors, DNA constructs, and recombinant host cells comprising said nucleic acid fragments.

Abstract: A pharmaceutical formulation comprising a growth hormone and leucine shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Abstract: The invention is directed to an isolated nucleic acid construct(s) comprising a nucleic acid sequence encoding an alkaline protease having a molecular weight of about 34 kD and is obtainable from a strain of Bacillus sp. Group I, as well as recombinant vectors and host cells comprising such constructs. Additionally, the invention is directed to a method for obtaining the protease. The invention is also directed to promoter and signal sequences derived from said alkaline protease as well as methods of using the promoter and signal sequences in the expression of heterologous nucleic acid sequences encoding heterologous proteins in bacteria.

Abstract: Fungicidal compositions comprising compounds of the general formula III ##STR1## cyclo-[Pec-MeAsp-MeVal-Val-MeVal-MeIle-Gly-MeVal-TyrOMe-D-Lact] (III) wherein each amino acid residue and the lactate residue independently may occur in L- or D-form, and derivatives thereof in combination with other biocidal agents are disclosed. Said compositions may be used for controlling fungi in crops and in the preservation of wood, paints, cosmetics, and edible products.

Abstract: The invention is directed to compounds having general formula (I) or general formula (II). Compounds of formulae (I) or (II) have interesting antifungal activities and may, accordingly, be used as active ingredients in fungicidal compositions.

Abstract: Novel compounds of the general composition I, Lactate (1), Glycine (1), Valine (1), Isoleucine (1), pipecolic acid (1), Aspanic acid (1), Tyrosine (1), wherein each amino acid residue independently may occur in L- or D- form, and wherein the number in parenthesis indicates the number of occurrences of each moiety, and derivatives thereof are disclosed. The compounds are producible by aerobic cultivation on suitable nutrient media under suitable conditions of a strain of the fungus Culvularia sp., subsequent recovery of the active component from the fermentation medium, and optionally modifying the active compound to obtain a compound of the desired general composition. Disclosed are also microorganisms capable of producing said compounds, compositions containing said compounds, and the use of such compositions for controlling fungi in crops, and in the preservation of wood, paints, cosmetics, and edible products.

Abstract: A pharmaceutical formulation comprising a growth hormone and isoleucine as additive or buffering substance shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Abstract: A variant of the C-terminal Kunitz-type protease inhibitor domain of the .alpha.3 chain of human type VI collagen, the variant comprising the following amino acid sequence X.sup.1 X.sup.16 Asp Ile Cys Lys Leu Pro Lys Asp X.sup.2 Gly X.sup.3 Cys X.sup.4 X.sup.5 X.sup.6 X.sup.7 X.sup.8 X.sup.9 Trp Tyr Tyr Asp Pro Asn Thr Lys Ser Cys Ala Arg Phe X.sup.10 Tyr Gly Gly Cys X.sup.11 X.sup.12 X.sup.13 Glu Asn Lys Phe X.sup.14 Ser Gln Lys Glu Cys Glu Lys Val Cys Ala Pro X.sup.15 (SEQ ID NO. 1) wherein X.sup.1, X.sup.15, and X.sup.16 represents a naturally occurring amino acid residues except Cys and X.sup.2 -X.sup.14 each independently respresents a naturally occurring amino acid residue, with the proviso that at least one of the amino acid residues X.sup.1 -X.sup.16 is different from the corresponding amino acid residue of the native sequence. Alternatively, the N-terminal Asp may be preceded by H or 3-5 amino acid residues and the C-terminal Pro may be followed by OH or 3-5 amino acid residues.