Amylolytic Enzymes Purification
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. Propriedades físico-químicas do amido isolado, estudo de parâmetros enzimáticos durante o armazenamento e caracterização de enzimas amilolíticas em raízes de maca (Lepidium meyenii Walp) / Physico-chemical properties of isolated starch, enzymatic parameters during storage, and characterization of amylolytic enzymes of maca (Lepidium meyenii Walp.) root
A maca (Lepidium meyenii Walpers) é uma planta herbácea bienal da família Brassicae, cultivada principalmente na região dos Andes da América do Sul. A parte subterrânea vem sendo consumida por muito tempo devido a seu valor nutricional e energético, mas é mais conhecida no mercado peruano e internacional por alegadas propriedades terapêuticas. Esta
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 05/07/2010
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2. Caracterização físico-química e purificação de enzimas amilolíticas de mandioca (Manihot esculenta Crantz) cv. Zolhudinha / Characterization physical-chemistry and purification of amylolytic enzymes from cassava (Manihot esculenta Crantz) cv.Zolhudinha
Cassava (Manihot esculenta Crantz) is a root from a native plant, cultivated in South América, that is hightly perish on the post-harvest time. The mechanisms of the root deterioration are due to enzymatic and oxidative reactions as well as the microbiological attack. In this work were studied roots of Zolhudinha variety, EMBRAPA - IM 158, cultivated in Ama
Publicado em: 2005
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3. Purification and Characterization of Extracellular Amylolytic Enzymes from the Yeast Filobasidium capsuligenum
The extracellular amylolytic system of Filobasidium capsuligenum consisted of an α-amylase (1,4-α-d-glucan glucanhydrolase, EC 3.2.1.1) and two forms of glucoamylase (1,4-α-d-glucan glucohydrolase, EC 3.2.1.3). The enzymes were purified by ammonium sulfate fractionation, repeated ion-exchange chromatography (DEAE-Sephadex A-50), and gel filtration (Sephad
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4. Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli.
The amylopullulanase gene (apu) of the thermophilic anaerobic bacterium Thermoanaerobacterium saccharolyticum B6A-RI was cloned into Escherichia coli. The complete nucleotide sequence of the gene was determined. It encoded a protein consisting of 1,288 amino acids with a signal peptide of 35 amino acids. The enzyme purified from E. coli was a monomer with an
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5. Macromolecular Structure and Morphology of Native Glycogen Particles Isolated from Candida albicans
A polysaccharide-rich particulate fraction was isolated from cytoplasmic extracts of Candida albicans by a procedure using differential centrifugation. The polysaccharide particles obtained after purification with deoxycholate treatment were essentially free of nitrogen and were identified chemically as polyglucosan, in which the glucosidic links were of alp
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6. Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115 degrees C.
Pyrococcus furiosus is a strictly anaerobic hyperthermophilic archaebacterium with an optimal growth temperature of about 100 degrees C. When this organism was grown in the presence of certain complex carbohydrates, the production of several amylolytic enzymes was noted. These enzymes included an alpha-glucosidase that was located in the cell cytoplasm. This
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7. A New Thermoactive Pullulanase from Desulfurococcus mucosus: Cloning, Sequencing, Purification, and Characterization of the Recombinant Enzyme after Expression in Bacillus subtilis
The gene encoding a thermoactive pullulanase from the hyperthermophilic anaerobic archaeon Desulfurococcus mucosus (apuA) was cloned in Escherichia coli and sequenced. apuA from D. mucosus showed 45.4% pairwise amino acid identity with the pullulanase from Thermococcus aggregans and contained the four regions conserved among all amylolytic enzymes. apuA enco
American Society for Microbiology.
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8. Cloning of the aapT gene and characterization of its product, alpha-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601.
A thermophilic and alkaliphilic Bacillus sp. strain, XAL601, was isolated from soil. It produces a thermostable and alkaline-stable enzyme with both alpha-amylase and pullulanase activities. The alpha-amylase-pullulanase gene (aapT) from this Bacillus strain was cloned, and its nucleotide sequence was determined (GenBank accession number D28467). A very larg