Abstract
In order to purify proteinase from Lactobacillus delbrueckii subsp. bulgaricus, chromatography methods including ion-exchange and hydrophobic interaction were combined. Chromatographic conditions were structured and optimized. The final sample volume, flow rate, and length of gradient for anion exchange chromatography were 20 mL, 5 mL/min and 10 column volume length of gradient, in that order. Besides, the flow rate and length of gradient for hydrophobic interaction chromatography were 1 mL/min and 10 column volume. Proteinase was purified up to 43-fold with a specific activity of 54.4 U/mg protein, and the recovery of 46.6%. The molecular weight of the purified proteinase was about 40 kDa.
| Original language | English |
|---|---|
| Pages (from-to) | 1560-1567 |
| Number of pages | 8 |
| Journal | International Journal of Food Properties |
| Volume | 18 |
| Issue number | 7 |
| DOIs | |
| State | Published - 3 Jul 2015 |
Keywords
- Hydrophobic interaction chromatography
- Ion-exchange chromatography
- Lactobacillus delbrueckii subsp. bulgaricus
- Proteinase
- Purification
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