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• W2068799057 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." @default.
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• W2068799057 date "2014-10-15" @default.
• W2068799057 modified "2023-10-17" @default.
• W2068799057 title "<i>Lactobacillus delbrueckii</i>subsp.<i>bulgaricus</i>Proteinase: Purification by Ion-Exchange and Hydrophobic Interaction Chromatography" @default.
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• W2068799057 doi "https://doi.org/10.1080/10942912.2014.921199" @default.
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