Bacterial and archaeal alpha-amylases
OwnerCharles F. Rice, Christopher J. Freeman +5inventors
InventorsCharles F. Rice, Christopher J. Freeman, Hannah Green, Aaron Argyros, Alexandra-Elena Panaitiu, Ryan Skinner, Anne K. Woodbrey
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Abstract
The present disclosure concerns an enzyme combination comprising at least one archaeal alpha-amylase and at least one bacterial alpha-amylase that can be used for the hydrolysis of a starchy biomass as well as the production of a fermentation product. The present disclosure also concerns variant polypeptides having alpha-amylase activity exhibiting higher enzymatic activity, lower dependence on the presence of a metallic ion, higher thermostability and/or higher resistance to chelation.
Claims29
An enzyme combination comprising at least one archaeal alpha-amylase and at least one bacterial alpha-amylase.
-24. (canceled)
-30. (canceled)
A population of recombinant microbial host cells comprising a first subpopulation of recombinant microbial host cells capable of expressing at least one archaeal alpha-amylase and a second subpopulation of recombinant microbial host cells capable of expressing at least one bacterial alpha-amylase.
-37. (canceled)
-41. (canceled)
A process for making an hydrolyzed liquefaction medium, the process comprising (i) contacting an untreated liquefaction medium with at least one archaeal alpha-amylase and at least one bacterial alpha-amylase and (ii) hydrolyzing the untreated liquefaction medium to generate the hydrolyzed liquefaction medium.
-49. (canceled)
-54. (canceled)
A variant polypeptide having alpha-amylase activity, wherein the variant polypeptide has at least 70% identity and less than 100% identity to the amino acid sequence of SEQ ID NO:
- 13, and is less dependent on the presence of a metallic ion, more thermostable and/or more resistant to chelation than the polypeptide consisting of the amino acid sequence of SEQ ID NO:
- 13.
-62. (canceled)
(canceled)
A variant polypeptide having alpha-amylase activity, wherein the variant polypeptide has at least 70% identity and less than 100% identity with the amino acid sequence of SEQ ID NO:
- 39, and is less dependent on a metallic ion, more thermostable and/or more resistant to chelation than the polypeptide consisting of the amino acid sequence of SEQ ID NO:
- 39.
-73. (canceled)
(canceled)
Dependencies are inferred from the claim text.