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. 2014 Dec 8;15(12):22678–22693. doi: 10.3390/ijms151222678

Figure 7.

Figure 7

In vitro protease activity of recombinant Sll0528. (a) The time-dependent proteolytic activity of recombinant Sll0528. Lane 1, the substrate beta-casein remained intact in the reaction buffer after 15 h of incubation. Lane 2, reaction mixture of GST-Sll0528 and beta-casein prior to incubation. Lanes 3 and 4, incubated with GST-Sll0528 for 5 and 15 h, the substrate beta-casein was cleaved significantly. Stars indicated the cleaved fragments of beta-casein; (b) The inhibitor study. Lane 1, GST-Sll0528 cleaved beta-casein significantly after 15 h incubation. Lane 2, the proteolytic activity of Sll0528 was not inhibited by Complete EDTA-free (a cocktail of serine and cysteine protease inhibitors). Lane 3, the proteolytic activity of Sll0528 was inhibited by 10 mM o-phenanthroline; (c) The comparison of proteolytic activity to the recombinant protein P. Lane 1, GST-Sll0528 cleaved beta-casein significantly after 15 h incubation. Lane 2, the substrate beta-casein remained intact in the reaction buffer after 15 h of incubation. Lane 3, purified GST-Sll0528 in the reaction buffer after 15 h incubation. Lane 4, reaction mixture of beta-casein and GST-recombinant protein P (indicated by triangle).