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Properties of three purified alpha-amylases from malted finger millet (ragi, Eleusine coracana, Indaf-15).
| Content Provider | CSIR - Central Food Technological Research Institute (CFTRI) |
|---|---|
| Author | Nirmala, M. Muralikrishna, G. |
| Abstract | Three alpha-amylases (EC 3.2.1.1) purified from ragi (Eleusine coracana, cv. Indaf-15) malt were investigated for their stability at different pH, temp. and concn. of CaCl2, EDTA, citric acid and oxalic acid. The enzymes (designated as alpha-1b, alpha-2 and alpha-3) were more stable at alkaline than acid pH, and were completely inactivated at pH 4.0. Both alpha-1b and alpha-3 retained 85% of their thermal stability after 15 min of heat treatment at 55C, whereas alpha-2 was completely inactivated; all 3 enzymes were inactivated at 75C, but thermal stability was enhanced by the presence of 5-7.5mM CaCl2. Enzyme activity was competitively inhibited by EDTA at mumol concn. in a temp. dependent manner, and both citric and oxalic acids completely inhibited the enzymes at concn. between 10 and 12.5mM. |
| Starting Page | 43 |
| Ending Page | 50 |
| Page Count | 8 |
| File Format | |
| Journal | Carbohydrate Polymers. |
| Volume Number | 54 |
| Issue Number | 1 |
| Language | English |
| Access Restriction | Authorized |
| Subject Keyword | Enzyme Biochemistry Ragi (Finger Millet) |
| Content Type | Text |
| Resource Type | Article |
