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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: High-level expression and characterization of a novel cutinase from Malbranchea cinnamomea suitable for butyl butyrate production

Fig. 2

Time course of recombinant cutinase produced by P. pastoris in a 5-L fermentor (a), and SDS-PAGE analysis of expression (b) and purification steps (c). The enzyme activity (filled triangle) and protein concentration (filled square) were monitored during high-cell density cultivation. The cutinase activity was determined at 45 °C in 50 mM Tris–HCl (pH 8.0) using pNPB as the substrate. All data are mean values of triplicate measurements. In b, lane M: low-molecular weight standard protein markers; lane 1: before methanol induction; lanes 2–8: culture supernatant collected after 12, 36, 60, 84, 108, 120, 132, and 144 h of methanol induction, respectively. In c, lane M: low-molecular weight standards; lane 1: crude enzyme; lane 2: purified enzyme

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