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: Novel compounds of the general composition I, Lactate (1), Glycine (1), Valine (4), Isoleucine (1), pipecolic acid (1), Aspartic 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 Curvularia 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: An endoprotease preparation, comprising an isolated endoprotease is disclosed. The endoprotease is a serine protease, shows immunochemical idenity to a protease derived from Fusarium oxysporum DSM 2672, hydrolyzes the oxidized beta-chain of bovine insulin at the peptide bonds Arg (22)-Gly (23) and Lys (29)-Ala(30), has optimum activity towards casein in the pH range of 8.5-11.0 with nearly constant activity in the pH range, has optimum activity at a temperature of about 45.degree. C., and has an isolectric point of about 9.0-10.0. The preferred microorganism that the enzyme is isolated from is Fusarium oxysporum DSM 2672.

Abstract: Combinations of alkaline Bacillus protease with alkaline fungal or actinomycete protease show improved detergency. Proteases obtainable from Fusarium sp. or Paecilomyces sp. (fungal) and Nocardiopsis sp. (actinomycete) are preferred.

Abstract: A process for recovering purified vegetable protein particularly soymeal protein by enzymatic treatment to dissolve the remanence employing a novel enzyme composition agent adapted to decompose a hitherto unreported pectic-like polysaccharide capable of binding to proteins. The process can recover protein from corn gluten, cotton seed meal, sunflower meal, rape meal etc.

Abstract: Purified vegetable protein particularly from soymeal produced by enzymatic treatment to dissolve the remanence employing a novel enzyme composition agent adapted to decompose a hitherto unreported pectic-like polysaccharide capable of binding to proteins.

Abstract: SPS--A novel pectic-like polysaccharide derived from soy plant cell walls characterized by capability to bind to proteins.SPS-ase--The carbohydrase complex capable of decomposing SPS into decomposition products incapable of attaching to protein, and method for producing SPS-ase by cultivation of an SPS-ase producing microorganism for which preferred microorganism strains are Aspergillus aculeatus CBS 101.43 and Aspergillus japonicus IFO 4408.

Abstract: Hydrolysis of plant kingdom polysaccharides by treatment with SPS-ase preparations.SPS-ase is an enzyme adapted to hydrolyzing the water-soluble protein binding polysaccharide present in soy flour decomposed by use of conventional pectinases, which polysaccharide is believed to be widespread in plant kingdom substances. Treatment with an SPS-ase preparation can clarify juices, wines and beers, hydrolyze process wastes such as sugar beet pulp, pomace, and soy milk remanence, improve the digestability of silage, and reduce the viscosity of wort.

Abstract: A harshness reducing, enzymatic additive for a main wash detergent based on a fungal cellulase, i.e., a cellulase produced by means of Humicola insolens. The enzymatic additive can be produced in high yields and has an extraordinarily high activity at alkaline pH values, whereby it is possible to mix the additive with a main wash detergent and perform the harshness reduction and the washing as a single operation.