AR011983A1 - KERATINOLYTIC PROTEASE EK3 AND XANTHOMONAS MALTHOPILIA EK3. - Google Patents

KERATINOLYTIC PROTEASE EK3 AND XANTHOMONAS MALTHOPILIA EK3.

Info

Publication number
AR011983A1
AR011983A1 ARP980101139A ARP980101139A AR011983A1 AR 011983 A1 AR011983 A1 AR 011983A1 AR P980101139 A ARP980101139 A AR P980101139A AR P980101139 A ARP980101139 A AR P980101139A AR 011983 A1 AR011983 A1 AR 011983A1
Authority
AR
Argentina
Prior art keywords
activity
protease
keratinolytic
malthopilia
xanthomonas
Prior art date
Application number
ARP980101139A
Other languages
Spanish (es)
Original Assignee
Procter & Gamble
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Procter & Gamble filed Critical Procter & Gamble
Publication of AR011983A1 publication Critical patent/AR011983A1/en

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20—Bacteria; Culture media therefor
    • C12N1/205—Bacterial isolates
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
    • C12R2001/00—Microorganisms ; Processes using microorganisms
    • C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
    • C12R2001/64—Xanthomonas

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Biotechnology (AREA)
  • Medicinal Chemistry (AREA)
  • Microbiology (AREA)
  • Biomedical Technology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Virology (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Molecular Biology (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

Proteasa que tiene una actividad queratinolítica. La proteasa tiene las siguientes propiedades físico químicas, (a) degrada caseínas y queratinasderivadas de cabello humano y animal. La actividad queratolitica es más elevada que la actividad ded egradacion de caseína; (b) muestra actividad máxima encondiciones alcalinas de pH 10, y aproximadamente un 60% de la actividad máxima en condiciones cercanas a las neutras (ph7); (c) retiene la actividadsustancialmente al 100% a ph 10 y el 70% aph 6-9, cuando se mantiene a 30sC durante 1 hora.Protease that has a keratinolytic activity. Protease has the following physical and chemical properties, (a) it breaks down caseins and keratins derived from human and animal hair. Keratolytic activity is higher than the casein degradation activity; (b) shows maximum activity in alkaline conditions of pH 10, and approximately 60% of the maximum activity in near neutral conditions (ph7); (c) retains activity substantially 100% at ph 10 and 70% aph 6-9, when maintained at 30sC for 1 hour.

ARP980101139A 1997-03-13 1998-03-13 KERATINOLYTIC PROTEASE EK3 AND XANTHOMONAS MALTHOPILIA EK3. AR011983A1 (en)

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP9059491A JPH10248564A (en) 1997-03-13 1997-03-13 Protease ek3 having keratin-degrading activity, and bacteria xanthomonas maltop hilia ek3 strain

Publications (1)

Publication Number Publication Date
AR011983A1 true AR011983A1 (en) 2000-09-13

Family

ID=13114826

Family Applications (1)

Application Number Title Priority Date Filing Date
ARP980101139A AR011983A1 (en) 1997-03-13 1998-03-13 KERATINOLYTIC PROTEASE EK3 AND XANTHOMONAS MALTHOPILIA EK3.

Country Status (4)

Country Link
JP (1) JPH10248564A (en)
AR (1) AR011983A1 (en)
AU (1) AU6110598A (en)
WO (1) WO1998040473A1 (en)

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AU5635300A (en) 1999-06-25 2001-01-31 Clorox Company, The Stain removing composition containing particular isolated and pure proteolytic enzymes
CA2377436A1 (en) * 1999-06-25 2001-01-04 The Penn State Research Foundation Low temperature enzymes derived from particular bacterial strain
US7319112B2 (en) 2000-07-14 2008-01-15 The Procter & Gamble Co. Non-halogenated antibacterial agents and processes for making same
US20050101002A1 (en) * 2003-11-06 2005-05-12 Council Of Scientific & Industrial Research Process for production of low temperature active alkaline protease from a deep-sea fungus

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH05211868A (en) * 1991-03-26 1993-08-24 Hokkaido Togyo Kk Production of alkali protease

Also Published As

Publication number Publication date
JPH10248564A (en) 1998-09-22
WO1998040473A1 (en) 1998-09-17
AU6110598A (en) 1998-09-29

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