DE945502T1 - Mutierte Subtilisin-protease - Google Patents
Mutierte Subtilisin-proteaseInfo
- Publication number
- DE945502T1 DE945502T1 DE0945502T DE99102452T DE945502T1 DE 945502 T1 DE945502 T1 DE 945502T1 DE 0945502 T DE0945502 T DE 0945502T DE 99102452 T DE99102452 T DE 99102452T DE 945502 T1 DE945502 T1 DE 945502T1
- Authority
- DE
- Germany
- Prior art keywords
- protease
- subtilisin
- mutation
- amino acid
- positions
- Prior art date
- Legal status (The legal status 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 status listed.)
- Pending
Links
- 108090000787 Subtilisin Proteins 0.000 title claims abstract 24
- 102000004190 Enzymes Human genes 0.000 claims abstract 8
- 108090000790 Enzymes Proteins 0.000 claims abstract 8
- 102200025035 rs786203989 Human genes 0.000 claims 48
- 102000035195 Peptidases Human genes 0.000 claims 47
- 108091005804 Peptidases Proteins 0.000 claims 47
- 239000004365 Protease Substances 0.000 claims 47
- 235000019419 proteases Nutrition 0.000 claims 47
- 102220528606 Ribonuclease P/MRP protein subunit POP5_S99D_mutation Human genes 0.000 claims 38
- 102220638186 Alkaline phosphatase, germ cell type_A98R_mutation Human genes 0.000 claims 36
- 102220204758 rs1057521825 Human genes 0.000 claims 35
- 230000035772 mutation Effects 0.000 claims 26
- 102220642080 Lipoma-preferred partner_N43R_mutation Human genes 0.000 claims 20
- 125000000539 amino acid group Chemical group 0.000 claims 17
- 102220245308 rs1555601006 Human genes 0.000 claims 12
- 102220341170 rs199565868 Human genes 0.000 claims 10
- 102220553651 Cyclic GMP-AMP synthase_S98D_mutation Human genes 0.000 claims 9
- 102220605934 Endoplasmic reticulum junction formation protein lunapark_T213D_mutation Human genes 0.000 claims 9
- 102200094890 rs121913565 Human genes 0.000 claims 9
- 108010056079 Subtilisins Proteins 0.000 claims 8
- 102000005158 Subtilisins Human genes 0.000 claims 8
- 102220076789 rs747976292 Human genes 0.000 claims 8
- 230000037431 insertion Effects 0.000 claims 7
- 238000003780 insertion Methods 0.000 claims 7
- 238000000034 method Methods 0.000 claims 7
- 102220481289 Podocan_R45A_mutation Human genes 0.000 claims 6
- 102220055690 rs727504021 Human genes 0.000 claims 6
- 102200093149 rs77938727 Human genes 0.000 claims 6
- 102200030534 rs36013132 Human genes 0.000 claims 5
- 102220096723 rs587778171 Human genes 0.000 claims 5
- 238000006467 substitution reaction Methods 0.000 claims 5
- 241000193830 Bacillus <bacterium> Species 0.000 claims 4
- 108010020132 microbial serine proteinases Proteins 0.000 claims 4
- 102220549033 B-cell linker protein_Y91F_mutation Human genes 0.000 claims 3
- 102220534200 B-cell lymphoma/leukemia 10_E53R_mutation Human genes 0.000 claims 3
- 102220493167 FGGY carbohydrate kinase domain-containing protein_N43K_mutation Human genes 0.000 claims 3
- 102200080006 rs118204447 Human genes 0.000 claims 3
- 102220093308 rs63751199 Human genes 0.000 claims 3
- 102220058097 rs730881898 Human genes 0.000 claims 3
- 102220285342 rs777971423 Human genes 0.000 claims 3
- 108010067770 Endopeptidase K Proteins 0.000 claims 2
- 101710173714 Subtilisin amylosacchariticus Proteins 0.000 claims 2
- ASCHNMXUWBEZDM-UHFFFAOYSA-N chloridodioxygen(.) Chemical compound [O]OCl ASCHNMXUWBEZDM-UHFFFAOYSA-N 0.000 claims 2
- 230000037430 deletion Effects 0.000 claims 2
- 238000012217 deletion Methods 0.000 claims 2
- 108010003855 mesentericopeptidase Proteins 0.000 claims 2
- 102220032359 rs104895271 Human genes 0.000 claims 2
- 102220279287 rs1554888120 Human genes 0.000 claims 2
- 102200033974 rs1555427497 Human genes 0.000 claims 2
- 108010031354 thermitase Proteins 0.000 claims 2
- 150000001413 amino acids Chemical class 0.000 claims 1
- 244000309464 bull Species 0.000 claims 1
- 230000007935 neutral effect Effects 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract 2
- 239000003599 detergent Substances 0.000 abstract 1
- 239000000203 mixture Substances 0.000 abstract 1
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)
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
-
- 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
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Peptides Or Proteins (AREA)
Claims (39)
1. Mutierte Subtilisin Protease, wobei die elektrostatische Nettoladung im Vergleich
zu der Ausgangsprotease bei gleichem pH verändert wurde, so dass es in der Protease,
relativ zu der Ausgangsprotease weniger oder mehr positiv-geladene(n) Aminosäurerest(e) gibt und/oder mehr oder weniger negativ-geladene(n) Aminosäurerest(e)
gibt, dadurch gekennzeichnet, dass mindestens eine Mutation von den Aminosäureresten an einer oder mehrerer der Positionen
1, 2, 3, 4, 10, 14, 15, 17, 18, 20, 40, 43, 44, 51, 52, 60, 61, 62, 91, 98, 100, 105,
106, 108, 112, 113, 117, 133, 134, 137, 141, 143, 144, 145, 146, 165, 167, 173,
183, 184, 185, 191, 192, 209, 210, 211, 212, 239, 240, 242, 243, 244, 245, 247,
248, 251, 252, 253, 255, 256, 257,259, 263, 269, 271, 272,
verursacht ist durch Deletion, Substitution oder Insertion (einfach oder mehrfach)
in Nachbarschaft zu den genannten Positionen, wobei die mutierte Subtilisin Protease
einen niedrigeren isoelektrischen Punkt (plo) hat als die Ausgangsprotease.
2. Mutierte Subtilisin Protease, wobei die elektrostatische Nettoladung im Vergleich
zu der Ausgangsprotease bei gleichem pH verändert wurde, so dass es in der Protease,
relativ zu der Ausgangsprotease weniger oder mehr positiv-geladene(n) Aminosäurerest(e) gibt und/oder mehr oder weniger negativ-geladene(n) Aminosäurerest(e)
gibt, dadurch gekennzeichnet, dass mindestens eine Mutation von den Aminosäureresten an einer oder mehreren der Positionen
1,2, 3,4,10,14,15,17,18,20,40,43, 44, 51, 52, 60, 61, 62, 91, 98,100,105,
106, 108, 112, 113, 117, 133, 134, 137, 141, 143, 144, 145, 146, 165, 167,173,
106, 108, 112, 113, 117, 133, 134, 137, 141, 143, 144, 145, 146, 165, 167,173,
DE/EP O 945502T1
-2-
183, 184, 185, 191, 192, 209, 210, 211, 212, 239, 240, 242, 243, 244, 245, 247,
248, 251,252, 253,255, 256,257,259,263,269, 271,272,
248, 251,252, 253,255, 256,257,259,263,269, 271,272,
verursacht ist durch Deletion, Substitution oder Insertion (einfach oder mehrfach)
in Nachbarschaft zu den genannten Positionen, wobei die Subtilisin Protease einen
höheren Isoelektrischen Punkt (plo) hat als die Ausgangsprotease.
3. Protease nach Anspruch 1 oder 2, dadurch gekennzeichnet, dass sie mindestens eine
Mutation besitzt, die einen Aminosäurerest beeinflusst, der eine Position besetzt,
ausgewählt aus der Gruppe von Positionen
1, 2, 3, 4, 10, 14, 15, 17, 18, 20, 40, 43, 44, 51, 52, 60, 61, 62, 91, 98, 100, 105,
106, 108, 112, 113, 117, 133, 134, 137, 141, 143, 144, 145, 146, 165, 167, 173, 183, 184, 185, 191, 192, 209, 210, 211, 212, 239, 240, 242, 243, 244, 245, 247,
248,251,252,253,255,256,257,259,263,269,271,272,
und mindestens eine weitere Mutation, die einen Aminosäurerest beeinflusst, der
eine Position besetzt, ausgewählt aus der Gruppe von Positionen
1, 2, 3, 4, 6, 9, 10, 12, 14, 15, 17, 18, 19, 20, 21, 22, 24, 25, 36, 37, 38, 40, 41, 43,.
44, 45, 46, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 75, 76, 77, 78, 79,
87, 89, 91, 94, 97, 98, 99, 100, 101, 103, 104, 105, 106, 107, 108, 109, 112, 113,
115, 116, 117, 118, 120, 126, 128, 129, 130, 131, 133, 134, 136, 137, 140, 141, 143, 144i 145, 146, 155, 156, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167,
170, 171, 172, 173, 181, 182, 183, 184, 185, 186, 188, 189, 191, 192, 194, 195,
197, 204, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 235, 236, 237, 238, 239, 240, 241, 242, 243, 244, 245, 247, 248, 249, 251, 252, 253, 254, 255,
256,257,259, 260, 261,262,263,265,269, 271, 272,275.
4. Mutierte Subtilisin Protease, wobei die elektrostatische Nettoladung im Vergleich
zu der Ausgangsprotease bei gleichem pH verändert wurde, dadurch gekennzeichnet,
dass sie eine oder mehrere der folgenden Mutationen enthält:
RlOF5RlOL,
DE/EPO 345.502 &Pgr;
-3-
RI0F+R45A+E89S+E136Q+R145A+D181N+R186P+E271Q, R10F+R19Q+E89S+E136Q+R145A+D181N+E271Q+R275Q,
Q12K,Q12R,
Q12K+P14D+T22K+N43R+Q59E+N76D+A98R+S99D+S156E+A158R+A172D+
N173K+T213R+N248D+T255E+S256K+S259D+A272R, Q12R+P14D+T22R+N43R+ Q59E+N76D+A98R+S99D+S156E+A158R+A172D+N173K+T213R+N248D+T255E+
S256K+S259D+A272R,Q12K+P14D+T22K+T38K+N43R+Q59E+N76D+A98R+
S99D+S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259+A272-R, Q12R+P14D+T22R+T38R+N43R+Q59E+N76D+A98R+S99D+S156E-
+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, Q12K+P14D+T22K+T3 8K+N43R+Q5 9E+N76D+A98R+S99D+H120D+N140D+S141R+
S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12R+P14D+T22R+T3 8R+N43R+Q59E+N76D+A98R+S99D+H120D+N140D+
S141R+S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D- +A272R,
P14K, P14K+*36D, P14K+N218D, P14K+P129D, A15K, A15R, R19Q, T22R,
D32*, *36D,
*36D+R170Y+G195E+K251E, *36D+H120D+R170Y+G195E+K235L, * 36D+H120D+R170 Y+G195E+K23 5L+K251E,
♦36D+H120D+G195E+K235L, T38K, T38R, N43R, N43K,
R45A, E53R, E53K, E53G+K235L, E54G, E54Y, Q59E, Q59E+N76D+A98R+S99D+S156E+A158R+A172D+N173K+T213R+N248D+T255E+-
S256K+S259D+A272R,
D60N, E89S, E89S+K251N, Y91F, G97D, G97D+H120K, A98K, A98R, S99D, S99D+N140K, E112T, H120K, H120D+K235L, H120D+G195E+K235L, H120D+R170Y+G195E+K235L, H120D+R170Y+G195E+K235L+R251E, P129D, E136Q, E136R, E136Q+R10L, N140D, N140K, N140R, S141K, SW IR, R145A, S156E, S156E+A158R+A172D+N173K, S156E+A158R+A172D+N173K+T213R, Sl 56E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, A158R, A158K, Y167V, R170Y+G195E, R170Y+K251E, R170Y+G195E+K251E, R170Y+G195E+K235L, Y171T, N173K, N184K,
D60N, E89S, E89S+K251N, Y91F, G97D, G97D+H120K, A98K, A98R, S99D, S99D+N140K, E112T, H120K, H120D+K235L, H120D+G195E+K235L, H120D+R170Y+G195E+K235L, H120D+R170Y+G195E+K235L+R251E, P129D, E136Q, E136R, E136Q+R10L, N140D, N140K, N140R, S141K, SW IR, R145A, S156E, S156E+A158R+A172D+N173K, S156E+A158R+A172D+N173K+T213R, Sl 56E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, A158R, A158K, Y167V, R170Y+G195E, R170Y+K251E, R170Y+G195E+K251E, R170Y+G195E+K235L, Y171T, N173K, N184K,
DE/ EP O 94 5 562 T1
N184R, N185D, R186P, Y192V, Y192V, Y192A, G195E+T213R, G195E+K251E, G195E+K235L, D197N, D197K, D197E,
Q206D, Q206E, Y209L, T213R, Y214T, Y214S, N218D, K235L, K235R,
K237R, W241Y, W241L, W241Y+H249R, W241L+H249R, N248D, K25IR,
K251E, K251N, T255E, S256R, S256K, S259L, S259D, Y263W, S265R, E271Q, E271G, E271G+K27V, E271Q E271G, A272R,
R275Q, D14K, D14K+D120K, D14K+D120K+D140K,
D14K+D120K+D140K+D172K,
E54T, E54Y, N97D, N97D+S98D, N97D+T213D, S98D, S98D+T213D,
D120K, D140K, S156E, D172K, T213D,N218D.
5. Mutierte Subtilisin Protease, dadurch gekennzeichnet, dass sie eine Insertionsmutation an Position 36 besitzt.
6. Protease nach Anspruch 5, dadurch gekennzeichnet, dass sie eine einen negativ
geladenen Aminosäurerest gebende Insertionsmutation an Position 36 besitzt.
7. Protease nach Anspruch 6, dadurch gekennzeichnet, dass die Mutation *36D oder
*36Eist.
8. Protease nach Anspruch 5, dadurch gekennzeichnet, dass die Insertionsmutation einen
neutralen Aminosäurerest zur Verfügung stellt.
9. Protease nach Anspruch 8, dadurch gekennzeichnet, dass die Mutation *36A, *36Q.
oder *36N ist.
10. Protease nach Anspruch 5, dadurch gekennzeichnet, dass die Insertionsmutation einen
positiv geladenen Aminosäurerest zur Verfügung stellt.
DE /EP O 94 5 5.02 Tl
11. Protease nach Anspruch 5, dadurch gekennzeichnet, dass die Mutation *36R oder
*36K ist.
12. Protease nach einem der Ansprüche 5 bis 11, dadurch gekennzeichnet, dass sie mindestens
eine weitere Mutation an mindestens einer der Positionen 120, 170, 195, 235, und 251 hat.
13. Protease nach Anspruch 12, dadurch gekennzeichnet, dass die Insertion *36D, *36E,
oder *36Q ist und die mindestens eine weitere Mutation ausgewählt ist aus H120D,
R170Y.G195E, K235L undK251E.
14. Protease nach einem der Ansprüche 5 bis 13, dadurch gekennzeichnet, dass sie eine
weitere Mutation an Position 76 besitzt.
15. Protease nach Anspruch 14, dadurch gekennzeichnet, dass die weitere Mutation dazu
da ist, einen negativ-geladenen Aminosäurerest in Position 76 zu ersetzen.
16. Protease nach Anspruch 15, dadurch gekennzeichnet, dass die weitere Mutation
N76D oder N76E ist.
17. Protease nach einem der Ansprüche 14 bis 16, dadurch gekennzeichnet, dass sie eine
weitere Mutation in mindestens einer oder mehr der Positionen 120, 170, 195, 235,
and 251 besitzt.
18. Protease nach Anspruch 17, dadurch gekennzeichnet, dass die genannte mindestens
eine weitere Mutation ausgewählt ist aus H120D, Rl 7OY, G195E, K235L und
K251E.
DE/EP O 94 5 502 TI
-6-
19. Protease nach einem der Ansprüche 5 bis 19, dadurch gekennzeichnet, dass sie eine
weitere Mutation besitzt, die anderswo in dem Proteasemolekül eine weitere positive
Ladung einfugt.
20. Protease nach Anspruch 19, dadurch gekennzeichnet, dass die weitere Mutation in
Position 213 ist.
21. Protease nach Anspruch 20, dadurch gekennzeichnet, dass die Mutation T213K ist.
22. Protease nach einem der vorangehenden Ansprüche, dadurch gekennzeichnet, dass
sie eine Mutation einer Ausgangsprotease darstellt, ausgewählt aus Subtilisin BPN',
Subtilisin amylosacchariticus, Subtilisin 168, Subtilisin Mesentericopeptidase, Subtilisin
Carlsberg, Subtilisin DY, Subtilisin 309, Subtilisin 147, Thermitase, Aqualysin,
Bacillus PB92 Protease, Proteinase K, Protease TW7 und Protease TW3.
23. Protease nach Anspruch 22, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin 309 ist.
24. Protease nach Anspruch 23, dadurch gekennzeichnet, dass sie irgendeine der folgenden
Substitutionen hat
RlOF5RlOL,
R10F+R45A+E89S+E136Q+R145A+D181N+R186P+E271Q,
R10F+R19Q+E89S+E136Q+R145A+D181N+E271Q+R275Q,
Q12K, Q12R,
Q12K+P14D+T22K+N43R+Q59E+N76D+A98R+S99D+S156E+A158R+A172D- +N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12K+P14D+T22K+N43R+Q59E+N76D+A98R+S99D+S156E+A158R+A172D- +N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12R+P14D+T22R+N43R+ Q59E+N76D+A98R+S99D+S156E+A158R+A172D-
+N173K+T213R+N248D+T255E+ S256K+S259D+A272R,
Q12K+P14D+T22K+T3 8K+N43R+Q59E+N76D+A98R+ S99D+S156E-
+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259+A272R,
+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259+A272R,
OE/EP 0 945502T1
-7-
Q12R+P14D+T22R+T38R+N43R+Q59E+N76D+A98R+S99D+S156E-
+Al 58R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12K+P14D+T22K+T38K+N43R+Q59E+N76D+A98R+S99D+H120D+N140D+S141R+ S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12R+P14D+T22R+T38R+N43R+Q59E+N76D+A98R+S99D+H120D+N140+S141R--S156E+A15
8R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
P14D, P14K, P14K+*36D, P14K+N218D, P14K+P129D, A15K, A15R, R19Q,
T22K, T22R, D32*, *36, *36D+R170Y+G195E+K251E, *36D+- H120D+R170Y+G195E+K235L, *36D+H120D+R170Y+G195E+K235L+K251E,
*36D+H120D+G195E+K235L, T38K, T38R, D41E, N43R, N43K, R45A, E53R, E53K, E53G+K235L, E54G, E54Y, Q59E,
Q59E+N76D+A98R+S99D+S156E+A158R+A172D+N173K+T213R+N248D+T255E+-
S256K+S259D+A272R,
D60N, N76D, E89S, E89S+K251N, Y91F, K94R, G97D, G97D+H120K, A98K, A98R, S99D, S99D+N140K, El 12T, H120K, H120D, H120D+K235L, H120D+G195E+K235L,H120D+R170Y+G195E+K235L, H120D+R170Y+G195E+K235L+K251E, P129D, E136Q, E136K, E136R, E136Q+R10L, N140D, N140K, N140R, S141K, S141R, R145A, S156E, S156E+A158R+A172D+N173K, S156E+A158R+A172D+N173K+T213R, S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, A158R, A158K, Y167V, R170Y+G195E, R170Y+K251E, R170Y+G195E+K251E, R170Y+G195E+K235L, Y171E, Y171T, A172D, N173K, D181N, N184K, N184R, N185D, R186P, Y192V, Y192V, Y192A, G195E+T213R, G195E+K251E, G195E+K235L, D197N, D197K, D197E, Q206D, Q206E, Y209L, T213R, T213K, Y214T, Y214S, N218D, K235L, K235R, K237R, W241Y5 W241L, W241Y+H249R, W241L+H249R, N248D, H249R, K251R, K251E, K251N, T255E, S256R, S256K, S259L, S259D, Y263W, S265K, S265R, E271Q, E271G, E271G+K27V, E271Q, E271G, A272R, A272R, R275Q.
D60N, N76D, E89S, E89S+K251N, Y91F, K94R, G97D, G97D+H120K, A98K, A98R, S99D, S99D+N140K, El 12T, H120K, H120D, H120D+K235L, H120D+G195E+K235L,H120D+R170Y+G195E+K235L, H120D+R170Y+G195E+K235L+K251E, P129D, E136Q, E136K, E136R, E136Q+R10L, N140D, N140K, N140R, S141K, S141R, R145A, S156E, S156E+A158R+A172D+N173K, S156E+A158R+A172D+N173K+T213R, S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, A158R, A158K, Y167V, R170Y+G195E, R170Y+K251E, R170Y+G195E+K251E, R170Y+G195E+K235L, Y171E, Y171T, A172D, N173K, D181N, N184K, N184R, N185D, R186P, Y192V, Y192V, Y192A, G195E+T213R, G195E+K251E, G195E+K235L, D197N, D197K, D197E, Q206D, Q206E, Y209L, T213R, T213K, Y214T, Y214S, N218D, K235L, K235R, K237R, W241Y5 W241L, W241Y+H249R, W241L+H249R, N248D, H249R, K251R, K251E, K251N, T255E, S256R, S256K, S259L, S259D, Y263W, S265K, S265R, E271Q, E271G, E271G+K27V, E271Q, E271G, A272R, A272R, R275Q.
25. Protease nach Anspruch 23 oder 24, dadurch gekennzeichnet, dass die Mutation
mindestens eine der folgenden ist:
DE/EP O 9455.02 Tl
-8-
-9-
DE/EP O 945 502 Tl
5202) N76D+G195E
5203) N76D+R17OY+G195E
5204) H120D+G195E+K235L+K251E
5223) Q59E+N76D+A98R+S99D+T213K+K235L+N248D+T255E- -S256K+S259D+A272R
5224) Q59E+N76D+A98R+S99D+H120D+N140D+S141R- +K235L+N248D+T255E+S256K+S259D+A272R
5225) ♦36D+Q59E+N76D+A98R+S99D+R170Y+S156E+A158R-
+A172D+N173R+K235L+N248D+T255E+S256K+S259D+A272R
S226) *36Q
5227) *36D+Q59E+N76D+A98R+S99D+H120D+N140D +S141R+R170Y+G195E+K235L+N248D+T255E-
+S256K+S259D+A272R
5228) *36D+Q59E+N76D+A98R+S99D+H120D+N140D+S141R+ S156E+A158R+A172D+N173K+K235L+N248D+-
T255E+S256K+S259D+A272R
5229) Q59E+N76D+A98R+S99D+H120D+N140D+S141R-
+S156E+A158R+A172D+N173K+K235L+N248D+T255E+- S256K+ 259D+A272R
S234) Q206D
S235) *36D+N76D
S242) *36Q+N76D+H120D+G195E+K235L
26. Protease nach Anspruch 22, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin 147 ist.
27. Protease nach Anspruch 22, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin Carlsberg ist.
28. Protease nach Anspruch 27, dadurch gekennzeichnet, dass sie eine der folgenden
Substitutionen hat:
D14K, D14K+D120K, D14K+D120K+D140K, D14K+D120K+D140K+D172K,
E54T, E54Y, N97D, N97D+S98D, N97D+T213D, S98D, S98D+T213D, D120K, D140K, S156E, D172K, T213D, N218D.
DE/EP O 945 5.02 &Tgr;1
-10-
29. Protease nach Anspruch 27 oder 28, dadurch gekennzeichnet, dass die Mutation eine
der folgenden ist:
COOl) D14K
C002) D120K
C003) D140K
C004) D14K+D120K
C008) D172K
C009) D14K+D120K+D140K
COlO) D14K+D120K+D140K+D172K
CO13) N97D.
CO14) S98D
C015) T213D
COl 7) S156E
CO18) N97D+S98D
CO19) N97D+T213D
C022) S98D+T213D
C028) N218D
ClOO) V51D
ClOl) E54T
C102) E54Y.
30. Protease nach Anspruch 22, dadurch gekennzeichnet, dass das Ausgangssubtilisin
die Bacillus PB92 Protease ist.
31. Protease nach Anspruch 30, dadurch gekennzeichnet, dass sie irgendeine der folgenden
Substitutionen hat
RlOF5RlOL, R10F+R45A+E89S+E136Q+R145A+D181N+R186P+E271Q,
R10F+R19Q+E89S+E136Q+R145A+D181N+E271Q+R275Q, Q12K, Q12R, Q12K+P14D+T22K+N43R+Q59E+N76D+A98R+S99D+S156E+A158R+A172D-
DE/EP O 94 5 5.02 Tl
-11-
+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12R+P14D+T22R+N43R+Q59E+N76D+A98R+S99D+S156&Egr;+&Agr;158R+A172D-
+N173K+T213R+N248D+T255E+S256K+S259D+A272R, Q12K+P14D+T22K+T38K+N43R+Q59E+N76D+A98R+S99D+S156E-
+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259+A272R, Q12R+P14D+T22R+T38R+N43R+Q59E+N76D+A98R+S99D+S156E-
+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
Q12K+P14D+T22K+T38K+N43R+Q59E+N76D+A98R+S99D+H120D+N140D+- S141R+S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+-
A272R,
Q12R+P14D+T22R+T38R+N43R+Q59E+N76D+A98R+S99D+H120D+N140+S141R—
S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R, P14D, &Rgr;14&Kgr;, P14K+*36D, P14K+N218D, P14K+P129D,
A15K, A15R, R19Q, T22K, T22R, D32*,
*36D, *36D+R170Y+G195E+K251E,
*36D, *36D+R170Y+G195E+K251E,
*36D+H120D+R170Y+G195E+K235L,
*36D+H120D+R170Y+G195E+K235L+K251E,
*36D+H120D+G195E+K235L,
T38K, T38R, D41E, N43R, N43K, R45A, E53R, E53K, E53G+K235L,
E54G, E54Y, Q59E,
Q59E+N76D+A98R+S99D+S156E+A158R+A172D+N173K+T213R+N248D+T255E^-
S256K+S259D+A272R,
D60N, N76D, E89S, E89S+K251N, Y91F, K94R, G97D,
G97D+H120K, A98K, A98R, S99D, S99D+N140K, El 12T, H120K,H120D,H120D+K235L,H120D+G195E+K235L,
H120D+R170Y+G195E+K235L,
H120D+R170Y+G195E+K235L+K251E,
P129D, E136Q, E136K, E136R, E136Q+R10L, N140D, NHOK, N140R,
SHlK, SHlR, R145A, S156E, S156E+A158R+A172D+N173K, S156E+A158R+A172D+N173K+T213R,
S156E+A158R+A172D+N173K+T213R+N248D+T255E+S256K+S259D+A272R,
A158R, A158K, Y167V, R170Y+G195E, R170Y+K251E, R170Y+G1-
-12-
DE/EP O 945502T1
95E+K251E, R170Y+G195E+K235L, Y171E, Y171T, A172D, N173K, D181N,
N184K, N184R, N185D, R186P, Y192V, Y192V, Y192A, G195E+T213R, G195E+K251E, G195E+K235L, D197N, D197K, D197E, Q206D, Q206E,
Y209L, T213R, T213K, Y214T, Y214S,N218D, K235L, K235R, K237R,
W241Y, W241L, W241Y+H249R, W241L+H249R, N248D, H249R, K251R,
K251E, K251N, T255E, S256R, S256K, S259L, S259D, Y263W, S265K,
S265R, E271Q, E271G, E271G+K27V, E271Q, E271G, A272R, A272R,
R275Q .
32. Protease nach Anspruch 30 oder 31, dadurch gekennzeichnet, dass die Mutation
mindestens eine der folgenden ist:
5004) R170Y+G195E
5005) K251E
5006) H120D
S008) H120D+G195E
5009) T71D
5010) T71D+G195E SOU) R170Y+K251E
S012) -R170Y+G195E+K251E S013) T71D+R170Y+K251E S014) T71D+R170Y+G195E+K251E
•S015) K235L
5016) H120D+K235L
5017) H120D+G195E+K235L SO 18) G195E+K251E
5019) H120D+R170Y+G195E+K235L
5020) H120D+R170Y+G195E+K235L+K251E
5021) *36D
5022) *36D+R170Y+G195E+K251E
S023) *36D+H120D+R170Y+G195E+K235L
5024) *36D+H120D+R170Y+G195E+K235L+K251E
5025) *36D+H120D+G195E+K235L
-13-
5026) E136R
5027) E89S
5028) D181N
5029) E89S+E136R SO3O) E89S+D181N
5031) D197N+E271Q
5032) D197N
5033) E271Q
SO35) *36D+N76D+H120D+G195E+K235L S041) G195F
5201) N76D
5202) N76D+G195E
5203) N76D+R170Y+G195E
5204) H12OD+G195E+K235L+K251E
S223) Q59E+N76D+A98R+S99D+T213K+K235L+N248D+T255E-
+S256K+S259D+A272R
5224) Q59E+N76D+A98R+S99D+H120D+N140D+S141R-
+K235L+N248D+T255E+S256K+S259D+A272R
5225) *36D+Q59E+N76D+A98R+S99D+R170Y+S156E+A158R-
+Al 72D+N173R+K235L+N248D+T255E+S256K+S259D+
A272R
5226) *36Q
5227) *36D+Q59E+N76D+A98R+S99D+H120D+N140D
+S141R+R170Y+G195E+K235L+N248D+T255E- +S256K+S259D+A272R
5228) *36D+Q59E+N76D+A98R+S99D+H120D+N140D+S141R+
S156E+A158R+A172D+N173K+K235L+N248D+-
T255E+S256K+S259D+A272R
S229) Q59E+N76D+A98R+S99D+H120D+N140D+S141R- +S156E+A158R+A172D+N173K+BC235L+N248D+T255E+-
S256K+ 259D+A272R S234) Q206D
- 14 -
S235) *36D+N76D
S242) ♦36Q+N76D+H120D+G195E+K235L.
33. Verfahren zur Bestimmung oder Selektion der in einem Ausgangsenzym zu deletierenden,
zu substituierenden oder zu inserierenden Position(en) und Aminosäure(n), dadurch gekennzeichnet, dass die Selektion in einer Weise durchgeführt wird, dass
die berechnete Nettoladung (=NEC) in einem erwägtem Mutanten-Enzym im Vergleich zu der NEC des Ausgangsenzyms der Wahl verändert wurde, berechnet bei
gleichem pH Wert und dass der ausgewählte Aminosäurerest aus den Aminonsäureresten
an irgendeiner oder mehreren der Positionen ausgewählt wird:
1, 2, 3, 4, 10, 14,15, 17, 18,20,40, 43, 44, 51, 52, 60, 61, 62, 91, 98, 100, 105, 106,
108, 112, 113, 117, 133, 134, 137,141, 143, 144, 145,146, 165, 167, 173, 183, 184,
185, 191, 192, 209, 210, 211, 212, 239, 240, 242, 243, 244, 245, 247, 248, 251, 252,
253, 255, 256, 257, 259, 263, 269, 271, 272,
34. Verfahren nach Anspruch 33, dadurch gekennzeichnet, dass die gewählte Aminosäurereste
so ausgewählt sind, dass sie einen Aminosäurerest bewirken, der eine der Positionen belegt ausgewählt aus der Gruppe von Positionen
1, 2, 3, 4, 10, 14, 15, 17, 18, 20, 21, 40, 43, 44, 49, 51, 52, 60, 61, 62, 91, 98, 100,
105, 106, 108, 112, 113, 117, 133, 134, 137, 141, 143, 144, 145, 146,165, 167, 173,
183, 184, 185, 191, 192, 209, 210, 211, 212, 239, 240, 242, 243, 244, 245, 247, 248,
251, 252, 253, 255, 256, 257, 259, 263, 269, 271, 272,
und mindestens ein weiterer bewirkt einen Aminosäurerest, der eine der Positionen
belegt, ausgewählt aus der Gruppe der Positionen:
1, 2, 3, 4, 6, 9, 10, 12, 14, 15, 17, 18, 19, 20, 21, 22, 24, 25, 36, 37, 38, 40, 41, 43,
44, 45, 46, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 75, 76, 77, 78, 79,
87, 89, 91, 94, 97, 98, 99, 100, 101, 103, 104, 105, 106, 107, 108, 109, 112, 113,
115, 116, 117, 118, 120, 126, 128, 129, 130, 131, 133, 134, 136, 137, 140, 141, 143,
144, 145, 146, 155, 156, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 170, 171,
172,173, 181, 182,183, 184, 185,186, 188, 189, 191,192, 194, 195,197, 204,206,
DE/EP 0
HL/ L. &igr; — -
-15-
209, 210, 211, 212, 213, 214, 215,216, 217, 218,235, 236, 237, 238, 239, 240, 241,
242, 243, 244, 245, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 259, 260, 261,
262,263,265,269,271,272,275.
35. Verfahren nach einem der Ansprüche 33 oder 34, dadurch gekennzeichnet, dass das
Ausgangsenzym ausgewählt ist aus Subtilisin BPN', Subtilisin amylosacchariticus,
Subtilisin 168, Subtilisin mesentericopeptidase, Subtilisin Carlsberg, Subtilisin DY,
Subtilisin 309, Subtilisin 147, Thermitase, Bacillus PB92 Protease, Proteinase K,
Protease TW7 und Protease TW3.
36. Verfahren nach Anspruch 35, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin 309 ist.
37. Verfahren nach Anspruch 35, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin 147 ist.
38. Verfahren nach Anspruch 35, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Subtilisin Carlsberg ist.
39. Verfahren nach Anspruch 35, dadurch gekennzeichnet, dass das Ausgangssubtilisin
Bacillus PB92 Protease ist.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DK316989A DK316989D0 (da) | 1989-06-26 | 1989-06-26 | Enzymer |
Publications (1)
Publication Number | Publication Date |
---|---|
DE945502T1 true DE945502T1 (de) | 2002-10-17 |
Family
ID=8119873
Family Applications (6)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
DE69034241T Expired - Lifetime DE69034241T2 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69034243T Revoked DE69034243T2 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69034266T Expired - Lifetime DE69034266D1 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69033644T Revoked DE69033644T2 (de) | 1989-06-26 | 1990-06-26 | Mutierte subtilisin-protease |
DE69034187T Expired - Lifetime DE69034187T2 (de) | 1989-06-26 | 1990-06-26 | Mutierte Subtilisin-protease |
DE0945502T Pending DE945502T1 (de) | 1989-06-26 | 1990-06-26 | Mutierte Subtilisin-protease |
Family Applications Before (5)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
DE69034241T Expired - Lifetime DE69034241T2 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69034243T Revoked DE69034243T2 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69034266T Expired - Lifetime DE69034266D1 (de) | 1989-06-26 | 1990-06-26 | Enzyme und Waschmittelzusammensetzungen |
DE69033644T Revoked DE69033644T2 (de) | 1989-06-26 | 1990-06-26 | Mutierte subtilisin-protease |
DE69034187T Expired - Lifetime DE69034187T2 (de) | 1989-06-26 | 1990-06-26 | Mutierte Subtilisin-protease |
Country Status (12)
Country | Link |
---|---|
EP (5) | EP1555314B1 (de) |
JP (3) | JP3343115B2 (de) |
KR (1) | KR100258459B1 (de) |
AT (5) | ATE362525T1 (de) |
AU (1) | AU5956690A (de) |
BR (1) | BR9007477A (de) |
CA (1) | CA2062732C (de) |
DE (6) | DE69034241T2 (de) |
DK (3) | DK316989D0 (de) |
ES (2) | ES2152209T3 (de) |
FI (3) | FI102907B1 (de) |
WO (1) | WO1991000345A1 (de) |
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DE4023458A1 (de) * | 1989-08-31 | 1991-03-07 | Kali Chemie Ag | Neue hochalkalische proteasen |
US6271012B1 (en) * | 1989-10-11 | 2001-08-07 | Genencor International, Inc. | Protease muteins and their use in detergents |
DK271490D0 (da) * | 1990-11-14 | 1990-11-14 | Novo Nordisk As | Detergentkomposition |
DE69130113T2 (de) * | 1990-12-05 | 1999-05-12 | Novo Nordisk A/S, Bagsvaerd | Proteine mit geänderten epitopen und verfahren zur deren herstellung |
ES2110488T3 (es) * | 1990-12-21 | 1998-02-16 | Novo Nordisk As | Mutantes enzimaticos con un bajo grado de variacion de la carga molecular en un intervalo de ph. |
US5482849A (en) * | 1990-12-21 | 1996-01-09 | Novo Nordisk A/S | Subtilisin mutants |
DE4106525A1 (de) * | 1991-03-01 | 1992-09-10 | Solvay Enzymes Gmbh & Co Kg | Verfahren zur verbesserung der stabilitaet von hochalkalischen proteasen |
EP0583339B1 (de) * | 1991-05-01 | 1998-07-08 | Novo Nordisk A/S | Stabilisierte enzyme und waschmittelzusammensetzungen |
ES2090481T3 (es) * | 1991-05-01 | 1996-10-16 | Unilever Nv | Composiciones detergentes que contienen enzimas estabilizadas. |
US5275945A (en) * | 1991-10-08 | 1994-01-04 | Vista Chemical Company | Alkaline proteases stable in heavy-duty detergent liquids |
HUT66846A (en) * | 1991-10-16 | 1995-01-30 | Unilever Nv | Aqueous enzymatic detergent compositions |
PL178045B1 (pl) * | 1992-07-17 | 2000-02-29 | Genencor Int | Mutant proteazy do stosowania w detergentach, sekwencja DNA kodująca mutanta proteazy, sposób otrzymywania mutanta proteazy oraz kompozycja detergentowa |
EP0663950B1 (de) * | 1992-10-06 | 2004-03-17 | Novozymes A/S | Zellulosevarianten |
DE4304161A1 (de) * | 1993-02-12 | 1994-08-25 | Solvay Enzymes Gmbh & Co Kg | Verbesserte hochalkalische Proteasen |
DK39093D0 (da) * | 1993-04-01 | 1993-04-01 | Novo Nordisk As | Enzym |
US6440717B1 (en) | 1993-09-15 | 2002-08-27 | The Procter & Gamble Company | BPN′ variants having decreased adsorption and increased hydrolysis |
US6436690B1 (en) | 1993-09-15 | 2002-08-20 | The Procter & Gamble Company | BPN′ variants having decreased adsorption and increased hydrolysis wherein one or more loop regions are substituted |
US5866526A (en) * | 1993-10-04 | 1999-02-02 | Novo Nordisk A/S | Enzyme preparation comprising a modified enzyme |
MA23346A1 (fr) | 1993-10-14 | 1995-04-01 | Genencor Int | Variantes de la subtilisine |
DE69432954T2 (de) * | 1993-10-14 | 2004-04-22 | The Procter & Gamble Company, Cincinnati | Proteasen enthaltende bleichmittelzusammensetzungen |
AU8079794A (en) * | 1993-10-14 | 1995-05-04 | Procter & Gamble Company, The | Protease-containing cleaning compositions |
EP1921148B1 (de) | 1994-02-24 | 2011-06-08 | Henkel AG & Co. KGaA | Verbesserte Enzyme und Detergentien damit |
ES2364774T3 (es) * | 1994-02-24 | 2011-09-14 | HENKEL AG & CO. KGAA | Enzimas mejoradas y detergentes que las contienen. |
US6110884A (en) * | 1994-03-29 | 2000-08-29 | Novo Nordisk A/S | Protease variants |
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-
1999
- 1999-01-08 FI FI990023A patent/FI112500B/fi not_active IP Right Cessation
-
2002
- 2002-03-04 JP JP2002057140A patent/JP3532902B2/ja not_active Expired - Lifetime
- 2002-03-04 JP JP2002057123A patent/JP2002315591A/ja active Pending
-
2003
- 2003-08-28 FI FI20031209A patent/FI20031209A/fi not_active Application Discontinuation
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