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Alpha-amylases

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20120270267 patent thumbnailZoom

Alpha-amylases


The present invention relates to alpha-amylase variants, polynucleotides encoding the variants and nucleic acid constructs, vectors, and host cells comprising the polynucleotides, and methods of using the variant enzymes.
Related Terms: Alpha-amylase

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Inventors: Carsten Andersen, Thomas Agersten Poulsen
USPTO Applicaton #: #20120270267 - Class: 435 696 (USPTO) - 10/25/12 - Class 435 
Chemistry: Molecular Biology And Microbiology > Micro-organism, Tissue Cell Culture Or Enzyme Using Process To Synthesize A Desired Chemical Compound Or Composition >Recombinant Dna Technique Included In Method Of Making A Protein Or Polypeptide >Blood Proteins

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The Patent Description & Claims data below is from USPTO Patent Application 20120270267, Alpha-amylases.

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REFERENCE TO SEQUENCE LISTING

This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference.

BACKGROUND OF THE INVENTION

1. Field of the Invention

The present invention relates to alpha-amylase variants, polynucleotides encoding the variants, methods of producing the variants, and methods of using the variants.

2. Description of Related Art

Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, E.C. 3.2.1.1) constitute a group of enzymes, which catalyze the hydrolysis of starch and other linear and branched 1,4-glucosidic oligo- and polysaccharides.

Alpha-amylases are used commercially for a variety of purposes such as in the initial stages of starch processing (e.g., liquefaction); in wet milling processes; and in alcohol production from carbohydrate sources. They are also used as cleaning agents or adjuncts in detergent matrices; in the textile industry for starch desizing; in baking applications; in the beverage industry; in oil fields in drilling processes; in recycling processes, e.g., for de-inking paper; and in animal feed.

One of the first bacterial alpha-amylases to be used was an alpha-amylase from B. licheniformis, also known as Termamyl™, which has been extensively characterized and the crystal structure has been determined for this enzyme. Alkaline amylases, such as the alpha-amylase derived from Bacillus sp. strains NCIB 12289, NCIB 12512, NCIB 12513, and DSM 9375 (disclosed in WO 95/26397), form a particular group of alpha-amylases that are useful in detergents. Many of these known bacterial amylases have been modified in order to improve their functionality in a particular application.

Termamyl™ and many highly efficient alpha-amylases require calcium for activity. The crystal structure of Termamyl™ shows that three calcium atoms are bound to the alpha-amylase structure coordinated by negatively charged amino acid residues. This requirement for calcium is a disadvantage in applications where strong chelating compounds are present, such as in detergents or during ethanol production from whole grains, where the plant material comprises a large amount of natural chelators such as phytate.

Calcium-insensitive amylases are known, e.g., the alpha-amylases disclosed in EP 1022334 and WO 03/083054, and a Bacillus circulans alpha-amylase having the sequence disclosed in UNIPROT:Q03657.

It would therefore be beneficial to provide alpha-amylases with reduced calcium sensitivity.

SUMMARY

OF THE INVENTION

The present invention provides alpha-amylase variants comprising an A-domain of a calcium-sensitive alpha-amylase, a B-domain which has at least 55% and less than 100% sequence identity with the B-domain of SEQ ID NO: 13, and a C-domain of a calcium-sensitive alpha-amylase.

The present invention also relates to isolated polynucleotides encoding an alpha-amylase variant, nucleic acid constructs, vectors, and host cells comprising the polynucleotides, and methods of producing a variant of a parent alpha-amylase.

The present invention also relates to the use of the variants in starch processing (e.g., liquefaction); wet milling processes; alcohol production from carbohydrate sources; detergents; dishwashing compositions; starch desizing in the textile industry; baking applications; the beverage industry; oil fields in drilling processes; recycling processes, e.g., for de-inking paper, and animal feed.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1 shows an alignment of SEQ ID NOS: 1-16, 29 and 30.

DETAILED DESCRIPTION

OF THE INVENTION

The present invention provides alpha-amylase variants comprising an A-domain of a calcium-sensitive alpha-amylase, a B-domain which has at least 50% and less than 100% sequence identity with the B-domain of SEQ ID NO: 13, and a C-domain of a calcium-sensitive alpha-amylase.

DEFINITIONS

A, B and C-Domains: The structure of alpha-amylases comprises three distinct domains A, B and C, see, e.g., Machius et al., 1995, J. Mol. Biol. 246: 545-559. The term “domain” means a region of a polypeptide that in itself forms a distinct and independent substructure of the whole molecule. Alpha-amylases consist of a beta/alpha-8 barrel harboring the active site, which is denoted the A-domain, a rather long loop between the beta-sheet 3 and alpha-helix 3, which is denoted the B-domain, and a C-domain and in some cases also a carbohydrate binding domain (e.g., WO 2005/001064; Machius et al., supra).



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stats Patent Info
Application #
US 20120270267 A1
Publish Date
10/25/2012
Document #
File Date
04/18/2014
USPTO Class
Other USPTO Classes
International Class
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Alpha-amylase


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