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Invertase Production by Fungi, Characterization of Enzyme Activity and Kinetic Parameters
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The present paper presents the results of research carried out on 14 fungal isolates of various origins aiming to select new efficient sources for invertase production for further biotechnological application. Aspergillus flavus presented the highest protein content and Aspergillus niger, the most intense invertase activity. The relationship between enzyme concentration and enzymatic activity at 0.25 mM mL-1sucrose as substrate assayed for successive decimal dilutions of Aspergillus niger enzyme ranging from 0.1 to 1mlLrevealed a linear correspondence between 0.1 and 0.5mL. The kinetic parameters Michaelis-Menten constant (Km) and maximal velocity (Vmax) for invertase activity of Aspergillus niger, Penicillium aurantiogriseum, Aspergillus wentii and Rhizopus stolonifer were calculated. The determination coefficients R2 calculated from Lineweaver-Burk plots presented values very close or equal to 1.
Revista de Chimie SRL
Title: Invertase Production by Fungi, Characterization of Enzyme Activity and Kinetic Parameters
Description:
The present paper presents the results of research carried out on 14 fungal isolates of various origins aiming to select new efficient sources for invertase production for further biotechnological application.
Aspergillus flavus presented the highest protein content and Aspergillus niger, the most intense invertase activity.
The relationship between enzyme concentration and enzymatic activity at 0.
25 mM mL-1sucrose as substrate assayed for successive decimal dilutions of Aspergillus niger enzyme ranging from 0.
1 to 1mlLrevealed a linear correspondence between 0.
1 and 0.
5mL.
The kinetic parameters Michaelis-Menten constant (Km) and maximal velocity (Vmax) for invertase activity of Aspergillus niger, Penicillium aurantiogriseum, Aspergillus wentii and Rhizopus stolonifer were calculated.
The determination coefficients R2 calculated from Lineweaver-Burk plots presented values very close or equal to 1.
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