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US 2014/0178962 A1Published application
Engineered carbonic anhydrase proteins for co2 scrubbing applications
AssigneeImiplex LLC
InventorsFrancis Raymond Salemme, Patricia C. Weber
Life of this patent
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Abstract
Engineered protein constructs with carbonic anhydrase catalytic activity, and their application in CO2 scrubbing.
Claims28
An engineered gamma carbonic anhydrase enzyme (gCA) polypeptide comprising
- residues 1-213 of Table 1, Sequence 1 (SEQ ID NO:
- 8) or a sequence greater than 90% identical thereto,
- residues 1-173 of Table 1, Sequence 4 (SEQ ID NO:
- 11) or a sequence greater than 90% identical thereto, or
- residues 1-181 of Table 1, Sequence 5 (SEQ ID NO:
- 12) or a sequence greater than 90% identical thereto.
3 more elements
(canceled)
An engineered gCA polypeptide comprising a polypeptide sequence of the form A(BDBD)vBC,
- wherein v is 0 or 1,
- wherein A is a sequence of Amino Terminus Sequence List A that is selected from the group consisting of
- no amino acid,
- HnXm, wherein X is any amino acid and m ranges from 0 to 20 and n ranges from 0 to 7 or from 4 to 7 (SEQ ID NO:
- 52), and
- LERAPGGLNDIFEAQKIEWHEXr (SEQ ID NO:
- 49), wherein each amino acid of the Xr subsequence is independently selected as any amino acid and r ranges from 0 to 7 or from 4 to 7,
- wherein B is a sequence of Sequence List B that is selected from the group consisting of SEQUENCES 9 through 41 of Table 2,
- wherein C is a sequence of Carboxy Terminus Sequence List C that is selected from the group consisting of
- no amino acid,
- XpHq, wherein X is any amino acid and p ranges from 0 to 20 and q ranges from 0 to 7 or from 4 to 7 (SEQ ID NO:
- 53), and
- XsLERAPGGLNDIFEAQKIEWHE (SEQ ID NO:
- 50), wherein each amino acid of the Xs subsequence is independently selected as any amino acid and s ranges from 0 to 7 or from 4 to 7,
- wherein D is a sequence of Sequence List D that is GaSbGcSd (SEQ ID NO:
- 51), wherein a, b, c, and d each independently range from 0 to 4.
13 more elements
(canceled)
-22. (canceled)
-27. (canceled)
A two-dimensional nanostructure, comprising:
- the di-biotin linked 2D hexagonal lattice on a fluid layer coated on a substrate,
- wherein each single chain gCA construct has a terminus,
- wherein the terminus of the single polypeptide chain of the single chain gCA construct comprises a polyhistidine,
- the fluid layer comprising a metal chelate,
- wherein the polyhistidine is bound to the metal chelate.
2 more elements
-31. (canceled)
A method, comprising:
- introducing a nucleotide sequence coding for an engineered gCA amino acid sequence having an Amino Terminal Biotinylation Sequence or a Carboxy Terminus Biotinylation Sequence into a host organism,
- culturing the host organism,
- lysing the host organism to release the engineered gCA amino acid sequence into a first solution,
- biotinylating the engineered gCA amino acid sequence,
- contacting the first solution with a substrate functionalized with an engineered avidin at a first pH, so that the biotinylated gCA amino acid sequence binds to the engineered avidin, and
- contacting the substrate with the engineered avidin with a second solution at a second pH, so that the engineered avidin releases the biotinylated gCA amino acid sequence in a purified form,
- wherein the Amino Terminal Biotinylation Sequence is LERAPGGLNDIFEAQKIEWHEXr (SEQ ID NO:
- 49), wherein each amino acid of the Xr subsequence is independently selected as any amino acid and r ranges from 0 to 7 or from 4 to 7, and
- wherein the Carboxy Terminal Biotinylation Sequence is. XSLERAPGGLNDIFEAQKIEWHE (SEQ ID NO:
- 50), wherein each amino acid of the XS subsequence is independently selected as any amino acid and s ranges from 0 to 7 or from 4 to 7.
7 more elements
(canceled)
Dependencies are inferred from the claim text.