| pubmed-article:8967771 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C0315087 | lld:lifeskim |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C0002245 | lld:lifeskim |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C0598079 | lld:lifeskim |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:8967771 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8967771 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8967771 | pubmed:dateCreated | 1996-12-19 | lld:pubmed |
| pubmed-article:8967771 | pubmed:abstractText | The extracellular alpha-amylase (1,4-alpha-D-glucanglucanohydrolase; EC 3.2.1.1) from Clostridium acetobutylicum ATCC 824 was purified to homogeneity by anion-exchange chromatography (mono Q) and gel filtration (Superose 12). The enzyme had an isoelectric point of 4.7 and a molecular weight of 84,000, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was a monomeric protein, the 19-amino-acid N terminus of which displayed 42% homology with the Bacillus subtilis saccharifying alpha-amylase. The amino acid composition of the enzyme showed a high number of acidic and hydrophobic residues and only one cysteine residue per mole. The activity of the alpha-amylase was not stimulated by calcium ions (or other metal ions) or inhibited by EDTA, although the enzyme contained seven calcium atoms per molecule. alpha-Amylase activity on soluble starch was optimal at pH 5.6 and 45 degrees C. The alpha-amylase was stable at an acidic pH but very sensitive to thermal inactivation. It hydrolyzed soluble starch, with a Km of 3.6 g . liter-1 and a Kcat of 122 mol of reducing sugars . s-1 . mol-1. The alpha-amylase showed greater activity with high-molecular-weight substrates than with low-molecular-weight maltooligosaccharides, hydrolyzed glycogen and pullulan slowly, but did not hydrolyze dextran or cyclodextrins. The major end products of maltohexaose degradation were glucose, maltose, and maltotriose; maltotetraose and maltopentaose were formed as intermediate products. Twenty seven percent of the glucoamylase activity generally detected in the culture supernatant of C. acetobutylicum can be attributed to the alpha-amylase. | lld:pubmed |
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| pubmed-article:8967771 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8967771 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8967771 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8967771 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8967771 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8967771 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8967771 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:8967771 | pubmed:author | pubmed-author:CrouxCC | lld:pubmed |
| pubmed-article:8967771 | pubmed:author | pubmed-author:GomaGG | lld:pubmed |
| pubmed-article:8967771 | pubmed:author | pubmed-author:SoucaillePP | lld:pubmed |
| pubmed-article:8967771 | pubmed:author | pubmed-author:PaquetVV | lld:pubmed |
| pubmed-article:8967771 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8967771 | pubmed:volume | 57 | lld:pubmed |
| pubmed-article:8967771 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8967771 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8967771 | pubmed:pagination | 212-8 | lld:pubmed |
| pubmed-article:8967771 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:meshHeading | pubmed-meshheading:8967771-... | lld:pubmed |
| pubmed-article:8967771 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:8967771 | pubmed:articleTitle | Purification and characterization of the extracellular alpha-amylase from Clostridium acetobutylicum ATCC 824. | lld:pubmed |
| pubmed-article:8967771 | pubmed:affiliation | Département de Génie Biochimique et Alimentaire, Centre National de la Recherche Scientifique Unité Associée 544, Toulouse, France. | lld:pubmed |
| pubmed-article:8967771 | pubmed:publicationType | Journal Article | lld:pubmed |
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