US2003022371A1PendingUtilityA1
Cold tolerances in plants
Priority: Jun 13, 1991Filed: Jul 27, 1999Published: Jan 30, 2003
Est. expiryJun 13, 2011(expired)· nominal 20-yr term from priority
Inventors:Marilyn Griffith
C07K 14/415C12N 9/2442C12Y 302/01039C12N 9/2437C12Y 302/01014C12Y 302/01004
23
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Cited by
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Claims
Abstract
A plurality of polypeptides derived from intercellular spaces of plant cells having frost tolerance. Some of the polypeptides are ice nucleators for developing ice crystals in extracellular spaces of plant tissue, some of the polypeptides are antifreeze components which control ice crystal growth in extracellular spaces and some of the polypeptides are enzymes which adapt plant cell walls to function differently during formation of ice crystals in plant intercellular spaces.
Claims
exact text as granted — not AI-modifiedI claim:
1 . Antifreeze polypeptides common to frost tolerant plants, said polypeptides being located in extracellular spaces of plant cells to control ice crystal growth in the intercellular plant space, such control of ice crystal growth providing a degree of plant frost tolerance
said polypeptides being selected from a group of polypeptides having respectively molecular weights of about 5 to 9 kD, about 9 to 11 kD, about 11 kD to 15 kD, about 21 to 23 kD, about 24 to 27 kD, about 30 to 31 kD, about 31 to 33 k0, about 32 to 36 kD, about 60 and 68 kD, about 89 to 100 kD and about 161 kD.
2 . A polypeptide of claim 1 wherein said selected polypeptide is further characterized by an amino acid residue content of the following respective listing:
Amino
93-99
Acid
11 kD
15 kD
23 kD
27 kD
31 kD
32 kD
33 kD
kD
ASX
8 4
15 8
11 7
11.6
11.6
14.6
12.3
5.6
GLX
8 3
6 5
8 6
6.9
8.8
7 3
8.3
12.5
SER
9 1
10.0
7 8
6.9
9.2
8.8
9.6
8.4
GLY
11.8
13.6
14 9
13.4
12.0
11.0
12.6
10.9
HIS
0.0
0.0
0.0
0.6
0.0
0.0
0.0
0.0
ARG
7.9
8.1
6.1
6.2
5.1
4.9
5.3
3.2
THR
8.8
9.3
11.8
9.5
6.0
6.2
7.2
5.4
ALA
14.2
8.2
8.8
11.5
12.5
11.7
10.1
9 0
PRO
9 3
6.4
9 3
5 4
6.7
7.6
7.1
16.7
TYR
2.7
2.5
2 6
5 2
3.8
4.9
4 8
2.7
VAL
4 8
3 9
4 4
4 9
5.3
5 3
5.3
3.9
MET
0.0
0 0
1.3
1.9
2.2
1.4
0.8
5.3
CYS
3.5
4.5
4 0
1.6
2.4
0.0
2.1
3.7
ILE
3 8
3.0
2.3
3.3
3.6
4.1
3.1
2.8
LEU
4.2
3 1
3.0
4.4
5.7
6.1
5.1
4.4
PHE
0.0
3 5
4 0
4.8
3.8
3.8
3.8
2.5
LYS
3 1
1 7
2.1
1.7
2.1
2.6
2.6
4.1
3 . A polypeptide of claim 2 wherein said selected 9 kD polypeptide is a lipid transfer protein and has an N-terminal amino acid sequence of:
NH 2 - ALA - ILE - PHE - CYS - CLY - GLN - VAL - ASN - PRO - ALA - LEU - GLY - PRO - PRO - ILE -TYR -
PRO - ALA - PHE - GLY.
4 . A polypeptide of claim 2 wherein said 11 kD polypeptide is a lipid transfer protein and has an N-terminal amino acid sequence of:
NH 2 - ALA - ILE - SER - X - GLY - GLU - GLN - VAL - ASN - SER - ALA - LEU - [GLY]- PRO - X - ILE -
[SER] - TYR - ALA - [ARG] - [GLY].
5 . A polypeptide of claim 2 wherein said selected 11 kD polypeptide is a thaumatin-like protein and has an N-terminal amino acid sequence of:
NH 2 - ARG - SER - PHE - SER - ILE - THR - ASN - ARG - CYS
-TRP - SER - PHE - THR - VAL - PRO - GLY.
6 . A polypeptide of claim 2 wherein said selected 15 kD polypeptide is a thaumatin-like protein and has an N-terminal amino acid sequence of:
NH 2 - ARG - SER - PHE - SER - ILE - THR - ASN - ARG - X -
ALA - PHE - THR - VAL - X - PRO - [ALA]- ALA - X -
[PRO]- VAL.
7 . A polypeptide of claim 2 wherein said selected 25 kD polypeptide has an N-terminal amino acid sequence of:
NH 2 - ALA - THR - ILE - THR - VAL - VAL - ASN - [LYS] -
PHE - SER - TYR - THR - VAL - X - PRO - GLY - ALA - LEU -
PRO - PHE - GLY - GLY - VAL - GLY - LEU - GLY - PRO - GLY
- GLN -
8 . A polypeptide of claim 2 wherein said selected 30 kD polypeptide is further characterized by an N-terminal amino acid sequence of:
NH 2 - ILE - GLY - VAL - CYS - TYR - GLY - VAL - ILE - GLY
- ASN - ASN - LEU - PRO - SER - ARG - SER - ASP - VAL -
VAL - GLN - LEU - TYR - ARG - SER - GLY - X - ILE - ASN - X
- MET -
wherein X indicates an unknown amino acid.
9 . A polypeptide of claim 2 wherein said selected 33 kD polypeptide has an N-terminal amino acid sequence of:
NH 2 - GLU - GLN - X - GLY - SER - GLN - ALA - GLY -
GLY - ALA - THR - X - PRO ASN - ASN - LEU - LEU -
wherein X indicates an unknown amino acid.
10 . A polypeptide of claim 9 wherein said polypeptide is a chitinase.
11 . A polypeptide of claim 1 wherein said polypeptide of selected molecular weight in the range of 31, 32 or 33 kD, is a glucanase.
12 . A polypeptide of claim 1 wherein said polypeptide of selected molecular weights in the range of 11 to 15 kD and 24 to 27 kD are thaumatin-like proteins.
13 . A polypeptide of claim 1 wherein said polypeptide of selected molecular weight in the range of 9 to 11 kD is a lipid transfer protein.
14 . A purified mixture of polypeptides derived from extracellular spaces of plant cells having frost tolerance and which induce frost tolerance in such plants, said composition comprising of a plurality of polypeptides, some of said polypeptides being ice nucleators for developing ice crystals in extracellular spaces of plant tissue, some of said polypeptides being antifreeze components which control ice crystal growth in extracellular spaces and at least one of said polypeptide being an enzyme which adapts plant cell walls to be flexible during formation of ice crystals in plant intercellular spaces, said purified mixture of polypeptides consisting of a group of polypeptides having molecular weights of about about 5 to 9 kD, about 9 to 11 kD, about 11 kD to 15 kD, about 21 to 23 kD, about 24 to 27 kD, about 30 to 31 kD, about 31 to 33 kD, about 32 to 36 kD, about 60 and 68 kD, about 89 to 100 kD and about 161 kD.
15 . A polypeptide mixture of claim 14 wherein said ice nucleating polypeptides have selected molecular weights in the range of 89 to 100 kD.
16 . A polypeptide composition of claim 15 wherein said antifreeze polypeptides have molecular weights of about about 5 to 9 kD, about 9 to 11 kD, about 11 kD to 15 kD, about 21 to 23 kD, about 24 to 27 kD, about 30 to 31 kD, about 31 go 33 kD, about 32 to 36 kD.
17 . In an immunoassay for determining if a plant is frost tolerant, the use of antibodies to one or more of said polypeptides of claim 1 to determine presence of antifreeze polypeptides, glucanases and ice nucleating polypeptides.
18 . A frozen food preparation including polypeptides of any one of claims 1 through 15.
19 . An ice cream preparation including polypeptides of any one of claims 1 through -15.
20 . A composition useful for inhibiting recrystallization of ice particles in biological matter or food product, said composition comprising at least one polypeptide selected from the group of antifreeze polypeptides having the molecular weight of about about 5 to 9 kD, about 9 to 11 kD, about 11 kD to 15 kD, about 21 to 23 kD, about 24 to 27 kD, about 30 to 31 kD, about 31 to 33 kD, about 32 to 36 kD, about 60 and 68 kD, about 89 to 100 kD and about 161 kD.
21 . A composition of claim 20 wherein antibodies to one or more of said polypeptides of claim 1 bound to said polypeptide enhance antifreeze activity.
22 . A method for inhibiting recrystallization of ice particles in biological matter or food product, said method comprising applying an effective amount of an antifreeze polypeptide selected from the group of antifreeze polypeptide having the molecular weights of about 5 to 9 kD, about 9 to 11 kD, about 11 kD to 15 kD, about 21 to 23 kD, about 24 to 27 kD, about 30 to 31 kD, about 31 to 33 kD, about 32 to 36 kD, about 60 and 68 kD, about 89 to 100 kD and about 161 kD.
23 . A method of claim 22 wherein said effective amount of antifreeze polypeptide is in the range of at least 25 μg of polypeptide per liter of contained water in said biological matter or food product.Join the waitlist — get patent alerts
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