Hybrid alpha-amylases are provided that share a conserved 3D structure in whole or in part with a wild-type Termamyl-like α-amylase, e.g., a Bacillus amylase. In the hybrid, an N-terminal portion of a Termamyl-like α-amylase is replaced with sequences from an archae α-amylase. The sequence similarity between the two amylase sequences may be less than 60%. Conserving the wild-type 3D structure in the hybrid facilitates obtaining enzymatically active amylases. In one embodiment, one or both amylase sequences contribute residues to the B domain, resulting in particularly advantageous properties. For instance, replacement of the Ca.sup.2+ binding site in the B domain of the Termamyl-like α-amylase with a B domain sequence of an archae α-amylase that does not bind Ca.sup.2+ can produce a hybrid that is fully active in the absence of Ca.sup.2+.

The present invention relates to alpha-amylase variants having an improved stability as compared to the parent alpha-amylase. The invention further relates to use of the variants, compositions comprising the variants, and methods of producing the variants.

The invention relates to liquid compositions, in particular for cleaning textiles, containing: (a) at least one surfactant, and (b) at least one α-amylase, which is at least 89% and increasing preferably at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and up to 100% identical to the sequence set forth in SEQ ID NO. 1 over the entire length thereof and has deletions at one or more of positions 180, 181, 182, 183, and 184 in the counting according to SEQ ID NO. 1, with the stipulation that the composition has a water activity (a.sub.w) between 0.3 and 0.95, in particular in a range of 0.4 to 0.95, at 25° C. and 1013 mbar, stabilize in particular the amylase.

The present invention relates to a method for identifying a pepsin resistant alpha amylase enzyme for use in a feed supplement comprising: i) providing an alpha amylase enzyme; ii) admixing said alpha amylase with com based feed and buffer solution comprising a pepsin concentration of 9000 U/ml at pH 3, 40° C., 500 rpm for al least 120 minutes and analysing alpha amylase activity on said alpha amylase compared to a control sample; wherein said control sample differs in that no pepsin is present during incubation; and iii) selecting an alpha amylase enzyme which substantially maintains alpha amylase activity under the assay conditions; feed supplements and feed stuffs comprising a pepsin resistant alpha amylase and the use of pepsin resistant alpha amylases in feed.

The disclosure encompassed herein relates, in part, to a method for increasing energy density of plant biomass that can be used for production of renewable fuel, such as biodiesel oil and/or ethanol. In an aspect, genetic engineering for enhanced sugar accumulation can be achieved by overexpressing a bacterial enzyme sucrose isomerase. Sugars or oils extracted from the plants of the disclosure encompassed herein may be used for industrial purposes such as heating, producing bio-fuels such as biodiesel fuel, or lubricating applications.

The present invention relates toalpha-amylasevariants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to an isolated synthetic polynucleotide encoding the mature amylase AX856 from Bacillus akibai, using codon modified polynucleotide constructs for the expression of the amylase.

Disclosed is a genetically recombinant Saccharomyces cerevisiae useful for degrading and utilizing kitchen wastes. Genes encoding α-amylase(AMY), glucoamylase (GA) and acid protease (AP) were introduced into the genetically recombinant Saccharomyces cerevisiae using a saccharomyces cerevisiae multi-gene co-expression vector and successfully expressed and secreted. The Saccharomyces cerevisiae so obtained are capable of secreting amylases and protease to degrade the starch and proteins in kitchen wastes to produce carbon and nitrogen sources such as glucose, polypeptides and amino acids, allowing fermentation into ethanol.

The present disclosure concerns the recombinant expression of thermostable alpha-amylases in a yeast host cell, compositions and yeast products made from the recombinant yeast host cells as well as the use of the thermostable alpha-amylase for hydrolyzing starch and ultimately making a fermentation product.

The present invention relates to variants of an alpha-amylase having improved stability to chelating agents relative to its parent enzyme, compositions comprising the variants, nucleic acids encoding the variants, methods of producing the variants, and methods for using the variants.