Endoprotease from Fusarium oxysporumDSM 2672 for use in detergents
AssigneeNovo Nordisk A/S
InventorsRuby I. Nielsen, Dorrit A. Aaslyng, Georg W. Jensen, Palle Schneider
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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.
Claims2
An endoprotease preparation, comprising an isolated endoprotease having the following characteristics:
- a) is a serine protease,
- b) shows immunochemical identity to a trypsin-like protease derived from Fusarium oxysporum DSM 2672 which hydrolyzes the oxidized beta-chain of bovine insulin at the peptide bonds Arg (22)-Gly (23) and Lys (29)-Ala(30),
- c) hydrolyzes the oxidized beta-chain of bovine insulin at the peptide bonds Arg (22)-Gly (23) and Lys (29)-Ala(30),
- d) has optimum activity towards casein in the pH range of 8.5-11 with nearly constant activity in said pH range,
- e) has optimum activity at a temperature of about 45.degree. C., and
- f) has an isolelectric point of about 9-10, wherein the preparation is devoid of other proteases.
Dependencies are inferred from the claim text.