AMY1, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
AMY1, subcloning in Escherichia coli strain DH5alpha, expression of the alpha-amylase C-terminally fused to the Aspergillus niger glucoamlyase starch binding domain in Aspergillus niger strain AB4.1, the mutant enzyme is secreted to the culture medium due to the signal peptide of the barley alpha-amylase
cloned in Escherichia coli DH5alpha and XL10-Gold to pPICZA-AMY1. pPICZA-AMY1 and the mutants Y105A/Y380A, Y105A/Y380M, H395A, Y380A/H395A, Y380A, Y380M, and Y105A are expressed in Pichia pastoris
cloning in Escherichia coli strain XL1-Blue and recombinant expression of His-tagged wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3)
cloning, isolation and characterization of members of the amylase gene family that are expressed in pancreas, Amy-2, and in the salivary gland and liver, Amy-1
coexpressed in a construct in Corynebacterium glutamicum, combined with Escherichia coli K-12 lysine decarboxylase for an one-step production of cadaverine. Construction of the Escherichia coli-Corynebacterium glutamicum shuttle vector, producing lysine decarboxylase under the control of the high constitutive expression promotor, and transformed this vector into Corynebaterium glutamicum. The engineered Corynebacterium glutamicum expresses both lysine decarboxlase and alpha-amylase, which retains their activity
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme lacking the native signal peptide in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression in Saccharomyces cerevisiae strain AH22, subcloning in Escherichia coli strain TG1
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of secereted His6-tagged mutant Gs4j-amyA N-terminally fused to OmpA signal peptide in Escherichia coli strain BL21(DE3) yielding 22fold increased enzyme production and activity as compared to the wild-type strain
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21T1R(DE3) with molecular chaperones plasmid pGro7 required for enzyme solubility, subcloning in Escherichia coli strain JM109
expression in Escherichia coli strain MK79, which also contains the hemoglobin gene from Vitreoscilla sp.. The hemoglobin gene enhances production of alpha-amylase
gene amy, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene amy-E, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene amy48, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of the extracellular fraction of enzyme TfAmy48 in Escherichia coli strain BL21(DE3)pLysS. The biochemical properties of the extracellular purified recombinant enzyme (rTfAmy48) are similar to those of the native one
gene amyA, sequence comparisons, recombinant overexpression in Escherichia coli strain BL21 (DE3) using the native signal peptide, method optimization leading to 8fold increased production of extracellular enzyme. The amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml
gene bllj_0710, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain MC1061
gene RB5AMG_01539, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RP
high level expression of thermostable Bacillus licheniformis alpha-amylase in Escherichia coli strain BL21-CodonPlus(DE3)-RIL mainly in inclusion bodies, subcloning in Escherichia coli strain DH5alpha
high level production in high-cell density culture of the food yeast Candida utilis. Expression of this synthetic gene under the control of the GAP promoter yields biologically active alpha-mylase, accounting for more than 50% of the soluble protein
high level recombinant expression in Pichia pastoris X-33 host strain using vector pGAPZaA, allowing constitutive expression and secretion of the protein
high level recombinant expression in Yarrowia lipolytica strain P01g using the vector pYLSC1 allowing constitutive expression and secretion of the protein
recombinant extracellular enzyme expression in Pichia pastoris strain GS115, highest alpha-amylase activity of 38314 U/ml is obtained with protein content of 28.7 mg/ml after 168 h high-cell density fermentation, the enzyme is secreted
sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3)
sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3) in inclusion bodies
the amplified 1.7 kb DNA fragment is inserted into an expression vector pBV220 to yield the recombinant plasmid pSBAM. The alpha-amylase gene in pSBAM is expressed in Escherichia coli. The production of the novel alpha-amylase activity reaches over 8 units/100 mL of the culture
transfer and heterologous expression of the gene in Xanthomonas campestris ATCC 13951. The transformed Xanthomonas produces similar levels of recombinant alpha-amylase activity, regardless of the carbon source present in growth medium, whereas the native Xanthomonas alpha-amylase production is highly dependent on starch availability and it is supressed in the presence of glucosse or other reducing sugars