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Jacaratia corumbensis O . Kuntze a New Vegetable Source for Milk-Clotting Enzymes
| Content Provider | Semantic Scholar |
|---|---|
| Author | Moreira, Keila Aparecida Cavalcanti, Maria Taciana Holanda Lima-Filho, José Figueiredo, Ana Porto |
| Copyright Year | 2009 |
| Abstract | The partial characterization and purification of mi lk clotting enzyme obtained from the (root latex) o f Jacaratia corumbensis O. kuntze was studied, by fractional pr eci itation with ammonium sulphate and ion exchange chromatography. The ammonium sulphate precipitate s howed five fractions (AS1– 0-20%; AS2 – 20-40%; AS3 – 4060%; AS4 – 60-80%; AS5 – 80-100%) and among the fra ctions obtained, the 40-60% fraction (AS3) showed t he highest milk clotting activity with a purification factor of 1.2 fold in relation to the crude extract . This fraction when applied on Mono Q column yielded two protein peaks (p1 and p2), but p1 pool showed the best milk-clott ing activity. The optimal pH for the crude and partially purified xtract was 6.5 and 7.0, respectively. The maximum ilk-clotting activity was at 55oC for the both crude and partial ly purified extracts. The enzyme was inhibited by i odoacetic acid which suggested that this enzyme was a cysteine pro t ase, with molecular weight of 33 kDa. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.scielo.br/pdf/babt/v52n1/a01v52n1.pdf |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | AS2 Eighty Ion Exchange Ion-Exchange Chromatography Procedure Ions Latex Milk (body substance) Molecular Weight Purification of quantum state Sulfate measurement Thioctic Acid ammonium lactate |
| Content Type | Text |
| Resource Type | Article |
