| pubmed-article:16850297 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16850297 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:16850297 | lifeskim:mentions | umls-concept:C0002245 | lld:lifeskim |
| pubmed-article:16850297 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:16850297 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16850297 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16850297 | pubmed:dateCreated | 2006-11-22 | lld:pubmed |
| pubmed-article:16850297 | pubmed:abstractText | A maltooligosaccharide-forming alpha-amylase was produced by a new soil isolate Bacillus subtilis KCC103. In contrast to other Bacillus species, the synthesis of alpha-amylase in KCC103 was not catabolite-repressed. The alpha-amylase was purified in one step using anion exchange chromatography after concentration of crude enzyme by acetone precipitation. The purified alpha-amylase had a molecular mass of 53 kDa. It was highly active over a broad pH range from 5 to 7 and stable in a wide pH range between 4 and 9. Though optimum temperature was 65-70 degrees C, it was rapidly deactivated at 70 degrees C with a half-life of 7 min and at 50 degrees C, the half-life was 94 min. The K (m) and V (max) for starch hydrolysis were 2.6 mg ml(-1) and 909 U mg(-1), respectively. Ca(2+) did not enhance the activity and stability of the enzyme; however, EDTA (50 mM) abolished 50% of the activity. Hg(2+), Ag(2+), and p-hydroxymercurybenzoate severely inhibited the activity indicating the role of sulfydryl group in catalysis. The alpha-amylase displayed endolytic activity and formed maltooligosaccharides on hydrolysis of soluble starch at pH 4 and 7. Small maltooligosaccharides (D2-D4) were formed more predominantly than larger maltooligosaccharides (D5-D7). This maltooligosaccharide forming endo-alpha-amylase is useful in bread making as an antistaling agent and it can be produced economically using low-cost sugarcane bagasse. | lld:pubmed |
| pubmed-article:16850297 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16850297 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16850297 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16850297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16850297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16850297 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16850297 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16850297 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16850297 | pubmed:issn | 0175-7598 | lld:pubmed |
| pubmed-article:16850297 | pubmed:author | pubmed-author:NagarajanDill... | lld:pubmed |
| pubmed-article:16850297 | pubmed:author | pubmed-author:RajagopalanGo... | lld:pubmed |
| pubmed-article:16850297 | pubmed:author | pubmed-author:KrishnanChand... | lld:pubmed |
| pubmed-article:16850297 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16850297 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:16850297 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16850297 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16850297 | pubmed:pagination | 591-7 | lld:pubmed |
| pubmed-article:16850297 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:meshHeading | pubmed-meshheading:16850297... | lld:pubmed |
| pubmed-article:16850297 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16850297 | pubmed:articleTitle | Purification and characterization of a maltooligosaccharide-forming alpha-amylase from a new Bacillus subtilis KCC103. | lld:pubmed |
| pubmed-article:16850297 | pubmed:affiliation | Department of Biotechnology, Indian Institute of Technology Madras, Chennai 600036, India. | lld:pubmed |
| pubmed-article:16850297 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16850297 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16850297 | lld:entrezgene |
