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Spectrophotometric determination of the kinetic parameters of β-fructofuranosidase and the mechanism of inhibition by copper (II) sulfate Zhang, Allen; Miao, Tyson
Abstract
Excessive dosages of heavy metals can be hazardous to organisms and the environment. This is due to the ability of heavy metal ions to inhibit several kinds of biological enzymes. In this experiment, the kinetic parameters of β-fructofuranosidase, a fungal enzyme that catalyzes the break-down of sucrose, were quantified through dinitrosalicylic acid assay and nonlinear regression. Furthermore, the activity of β-fructofuranosidase was measured in 6 different concentrations of copper (II) sulfate, an inhibitor, to determine the nature of inhibition. From the experiment, the results show that the nature of inhibition is noncompetitive at [CuSO₄] < 0.0022M and competitive at [CuSO₄] > 0.0044M, Vmax is 0.441 ± 0.0354mmol min, Km is 17.6 ± 2.6mM, and Ki is 0.00863 ± 0.00101.
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Title |
Spectrophotometric determination of the kinetic parameters of β-fructofuranosidase and the mechanism of inhibition by copper (II) sulfate
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Creator | |
Date Issued |
2011-04
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Description |
Excessive dosages of heavy metals can be hazardous to organisms and the environment. This is due to the ability of heavy metal ions to inhibit several kinds of biological enzymes. In this experiment, the kinetic parameters of β-fructofuranosidase, a fungal enzyme that catalyzes the break-down of sucrose, were quantified through dinitrosalicylic acid assay and nonlinear regression. Furthermore, the activity of β-fructofuranosidase was measured in 6 different concentrations of copper (II) sulfate, an inhibitor, to determine the nature of inhibition. From the experiment, the results show that the nature of inhibition is noncompetitive at [CuSO₄] < 0.0022M and
competitive at [CuSO₄] > 0.0044M, Vmax is 0.441 ± 0.0354mmol
min, Km is 17.6 ± 2.6mM, and Ki is 0.00863 ± 0.00101.
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Genre | |
Type | |
Language |
eng
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Series | |
Date Available |
2011-08-26
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Provider |
Vancouver : University of British Columbia Library
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Rights |
Attribution-NonCommercial-NoDerivatives 4.0 International
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DOI |
10.14288/1.0107229
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URI | |
Affiliation | |
Campus | |
Peer Review Status |
Unreviewed
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Scholarly Level |
Undergraduate
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DSpace
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Rights
Attribution-NonCommercial-NoDerivatives 4.0 International