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Fig. 5 | BMC Biotechnology

Fig. 5

From: A novel eurythermic and thermostale lipase LipM from Pseudomonas moraviensis M9 and its application in the partial hydrolysis of algal oil

Fig. 5

Characterization of LipM and effects of additives on LipM. a Specific activities of LipM towards p-NP esters of various chain lengths (C2, acetate; C4, butyrate; C8, caprylate; C10, decanoate; C12, laurate; C14, myristate; and C16, palmitate); b The pH profile of LipM. These relative activities of LipM were measured at different pH values. The enzyme activity in Tris-HCl (50 mM, pH 8.0) was taken as 100 %. Buffers used (final concentration 50 mM) were citrate-phosphate buffer (pH 4.0–6.5), Tris–HCl buffer (pH 7.0–8.5), and Glycine-NaOH buffer (pH 9.0–10.0); c Effect of temperature on the activity of LipR; d Thermal stability of LipM. The enzyme was incubated at 60 °C (■), 65 °C (), 70 °C (▲), 75 °C () and 85 °C () and for the indicated time

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