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1. WO1997030172 - COLD-ACTIVE PROTEASE CP-58 AND PSYCHROTROPHIC BACTERIA

Publication Number WO/1997/030172
Publication Date 21.08.1997
International Application No. PCT/US1997/002437
International Filing Date 14.02.1997
Chapter 2 Demand Filed 15.09.1997
IPC
C11D 3/386 2006.01
CCHEMISTRY; METALLURGY
11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
3Other compounding ingredients of detergent compositions covered in group C11D1/101
16Organic compounds
38Products with no well-defined composition
386Preparations containing enzymes
C12N 9/52 2006.01
CCHEMISTRY; METALLURGY
12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
9Enzymes, e.g. ligases (6.); Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating, or purifying enzymes
14Hydrolases (3.)
48acting on peptide bonds, e.g. thromboplastin, leucine aminopeptidase (3.4)
50Proteinases
52derived from bacteria
CPC
C11D 3/386
CCHEMISTRY; METALLURGY
11ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
DDETERGENT COMPOSITIONS
3Other compounding ingredients of detergent compositions covered in group C11D1/00
16Organic compounds
38Products with no well-defined composition ; , e.g. natural products
386Preparations containing enzymes ; , e.g. protease, amylase
C12N 9/52
CCHEMISTRY; METALLURGY
12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
9Enzymes; Proenzymes; Compositions thereof
14Hydrolases (3)
48acting on peptide bonds (3.4)
50Proteinases ; , e.g. Endopeptidases (3.4.21-3.4.25)
52derived from bacteria ; or Archaea
C12Y 304/00
CCHEMISTRY; METALLURGY
12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
YENZYMES
304Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
Applicants
  • THE PROCTER & GAMBLE COMPANY [US]/[US] (AllExceptUS)
  • JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY [JP]/[JP] (AllExceptUS)
  • HASAN, A., K., M., Quamrul [BD]/[JP] (UsOnly)
  • TAMIYA, Eiichi [JP]/[JP] (UsOnly)
Inventors
  • HASAN, A., K., M., Quamrul
  • TAMIYA, Eiichi
Agents
  • REED, T., David
Priority Data
8/2961616.02.1996JP
Publication Language English (EN)
Filing Language English (EN)
Designated States
Title
(EN) COLD-ACTIVE PROTEASE CP-58 AND PSYCHROTROPHIC BACTERIA
(FR) PROTEASE ACTIVE A FROID CP-58 ET BACTERIES PSYCHROTROPHES
Abstract
(EN)
A cold-active protease is here disclosed which has the following physicochemical properties: (a) specific activity and substrate specificity: the protease acts on casein, gelatin, albumin and hemoglobin to specifically decompose them in the order of casein, gelatin, albumin and hemoglobin; (b) optimal pH: 7.5 to 8.0; (c) pH stability: the protease is stable at a pH in the range of 5.5 to 10.5 at 20 °C for 1 hour; (d) optimal temperature: 20 °C at pH 10.5 and 40 °C at pH 8.0; (e) temperature stability: at pH 10.5 for 1 hour, the protease is scarcely inactivated at a temperature of 10 °C to 30 °C, but it is inactivated at 40 °C as much as about 30 % and completely inactivated at 50 °C; (f) enzyme activity: the protease has about 60 % or more of its maximum activity at 20 °C; (g) the active center of the enzyme is a metallic ion; and (h) the molecular weight of the protease is about 58 kDa as measured by SDS-PAGE.
(FR)
Cette protéase active à froid présente les propriétés physico-chimiques suivantes: (a) activité spécifique et spécificité de substrats: elle agit sur la caséine, la gélatine, l'albumine et l'hémoglobine en les décomposant, dans la spécificité décroissante de ces substrats; (b) pH optimum: 7,5 à 8; (c) stabilité selon pH: cette protéase est stable à un pH allant de 5,5 à 10,5 à 20 °C pendant une heure; (d) température optimum: 20 °C à un pH de 10,5 et 40 °C à un pH de 8; stabilité à la température: à un pH de 10,5 pendant une heure, la protéase est à peine inactivée à une température de 10 à 30 °C, mais elle l'est à 40 °C à raison de 30 % environ, et complètement à 50 °C; (f) activité enzymatique: cette protéase présente au moins 60 % de son activité maximum à 20 °C; (g) le centre actif de cette enzyme est un ion métallique; et (h) la masse moléculaire de la protéase est d'environ 58 kDa telle que mesurée par SDS-PAGE.
Also published as
Latest bibliographic data on file with the International Bureau