| Autor: |
Bagh, Antima Abasha, Ahlawat, Sushma, Verma, Yashodhara |
| Předmět: |
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| Zdroj: |
Biochemical & Cellular Archives; Oct2024, Vol. 24 Issue 2, p2507-2510, 4p |
| Abstrakt: |
Beta-galactosidase (EC 3.2.1.23), also known as lactase, is an exoglycosidase enzyme responsible for hydrolyzing the β-glycosidic bond between galactose and its organic moiety. This study focused on extracting, purifying, characterizing and immobilizing β-galactosidase from tomato leaves. The enzyme was successfully extracted using a 0.2 M sodium phosphate buffer at pH 6. To evaluate its chemical properties, the effects of temperature, pH, enzyme concentration and substrate concentration on enzyme activity were examined. The optimal temperature for β-galactosidase activity was found to be 50°C and the enzyme demonstrated the highest solubility at pH 6. The kinetic parameters of the free enzyme were determined, revealing a Michaelis constant (Km) of 0.1 mM and a maximum reaction velocity (Vmax) of 48.78 ìmol/min. These findings provide valuable insights into the enzyme's efficiency and behaviour under various conditions, which are essential for optimizing its application in industrial processes. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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