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_23
Snippet: Protease activity was assayed in supernatants of strain CECT 7210 grown in MRSC media containing glucose, lactose or maltose as sole carbon source, respectively (all of them at 20 g/L). Protease activity was measured in supernatants after 17 h of growth and centrifuged at 12,000 × g for 15 min under refrigerated conditions. BSA degradation (1% w/v, citrate-phosphate buffer 50 mM, pH 6.4) was measured at different incubation times (1 h, 3 h and 5.....
Document: Protease activity was assayed in supernatants of strain CECT 7210 grown in MRSC media containing glucose, lactose or maltose as sole carbon source, respectively (all of them at 20 g/L). Protease activity was measured in supernatants after 17 h of growth and centrifuged at 12,000 × g for 15 min under refrigerated conditions. BSA degradation (1% w/v, citrate-phosphate buffer 50 mM, pH 6.4) was measured at different incubation times (1 h, 3 h and 5 h) both with the supernatants and with 3 KDa concentrated fractions. Using the supernatants and the 3 KDa concentrated fractions, enzymatic reactions were performed with β-casein as substrate. Assays were performed as described above and β-casein degradation and 11-mer formation were monitored by HPLC.
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