AI Summary & Key Takeaways
AI InsightThe Km and Vmax values of the crude enzyme for p-nitrophenyl butyrate hydrolysis were found to be 7.15 mM and 7.067 mM/min, respectively.
📌 3 Key Takeaways
Abstract
This is the first report about the characterization of Trichoderma harzianum lipase. A novel strain of Trichoderma harzianum IDM14D was isolated from soil. The isolated strain was cultivated for lipase production in shake flasks at 30 °C for 7 days. For lipase production, it was determined that the best carbon source was glucose and the best nitrogen source was peptone. Maximum biomass was produced at a concentration of 1.25 g/L, in 7 days. The optimum pH and temperature for activity of the enzyme were 8.5 and 40 °C, respectively. The lipase was stable at a pH range of 8.0-10.0 and at 40 °C for 60 min. Ca2+ and Mn2+ enhanced lipase activity but it was determined that other metallic ions did not affect the enzyme activity. The Km and Vmax values of the crude enzyme for p-nitrophenyl butyrate hydrolysis were found to be 7.15 mM and 7.067 mM/min, respectively.
Özet
This is the first report about the characterization of Trichoderma harzianum lipase. A novel strain of Trichoderma harzianum IDM14D was isolated from soil. The isolated strain was cultivated for lipase production in shake flasks at 30 °C for 7 days. For lipase production, it was determined that the best carbon source was glucose and the best nitrogen source was peptone. Maximum biomass was produced at a concentration of 1.25 g/L, in 7 days. The optimum pH and temperature for activity of the enzyme were 8.5 and 40 °C, respectively. The lipase was stable at a pH range of 8.0-10.0 and at 40 °C for 60 min. Ca2+ and Mn2+ enhanced lipase activity but it was determined that other metallic ions did not affect the enzyme activity. The Km and Vmax values of the crude enzyme for p-nitrophenyl butyrate hydrolysis were found to be 7.15 mM and 7.067 mM/min, respectively.