| Autor: |
PANAJOTOVA, N., DOBREVA, V. T., ZHEKOVA, B. Y., DOBREV, G. T. |
| Předmět: |
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| Zdroj: |
Oxidation Communications; 2023, Vol. 46 Issue 3, p677-694, 18p |
| Abstrakt: |
An extracellular lipase was isolated and purified from the culture broth of Aspergillus carbonarius NRRL 369 by chromatographic techniques, resulting in a purification degree of 7-fold with a specific activity of 2.24 U/mg. The molecular weight was estimated by SDS-PAGE to be 187 kDa. The biochemical characteristics of the enzyme such as pH and temperature optimum and stability were analysed. Maximum lipase activity was observed in a wide range of temperatures and pH values with an optimum temperature of 40°C and pH of 6.0. The purified lipase was found to be thermostable in nature exhibiting high catalytic performance at pH 4 and about 75% residual activity present at 60°C. Metal ions such as Mn2+, Zn2+, Co2+, and Ca2+ increased lipase activity remarkably. Its marked stability and activity in organic solvents suggest that this lipase is highly suitable as a biotechnological tool with a variety of applications including organo-synthetic reactions, flavour compounds, and biodiesel production. The kinetics parameters of the purified enzyme were calculated to be Km = 1.24 mmol/l and Vmax = 0.036 U/ml, respectively. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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