Author: Chenoll, Empar; Casinos, Beatriz; Bataller, Esther; Buesa, Javier; Ramón, Daniel; Genovés, Salvador; Fábrega, Joan; Rivero Urgell, Montserrat; Moreno Muñoz, José A.
Title: Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity Document date: 2016_5_4
ID: 0sxl6f1r_21
Snippet: The hydrolysis was carried out in a solution containing 15 ml of protease-purified fraction (0.04 U), 30 mL of 2% β-casein solution (BioUltra, Sigma-Aldrich) and 105 mL phosphate citrate buffer (50 mM pH 6.4). After 48 h hydrolysis at 50 • C, samples were boiled for 10 min and peptides formation was analyzed by HPLC. Evaluation of 11-mer formation and β-casein degradation was conducted on a HPLC (Waters 2695) with photodiode array detector (W.....
Document: The hydrolysis was carried out in a solution containing 15 ml of protease-purified fraction (0.04 U), 30 mL of 2% β-casein solution (BioUltra, Sigma-Aldrich) and 105 mL phosphate citrate buffer (50 mM pH 6.4). After 48 h hydrolysis at 50 • C, samples were boiled for 10 min and peptides formation was analyzed by HPLC. Evaluation of 11-mer formation and β-casein degradation was conducted on a HPLC (Waters 2695) with photodiode array detector (Waters 2996) and C18 column (Sunfire Waters C18 5 mm 4.6 * 150 mm). Eluents were water (MilliQ quality; A) and acetonitrile (90% v/v; B), both with TFA 0.1% (v/v). Chromatographic conditions are summarized in Table 1 . Characterization of the Purified Protease
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