Biochemical Calculations I H Segel Wiley 1976 Pdf To Word
. 409 Downloads.SummaryThe rate of reducing sugars released through invertase activity exhibited a buffer pH optimum of 5.0.
Generally, the decline in invertase activity in its pH-profile near the optimal pH range was due to a reversible reaction that involved ionization or deionization of the functional groups in the active centre of the protein, but under highly acidic or alkaline conditions (pH9) the reduced activity appears to be due to irreversible inactivation of the enzyme. The dependence of the reaction on the amount of enzyme present was linear up to 3 g of soil. By varying the substrate concentration, it was found that the reaction rate of this enzyme approached zero-order kinetics when 145m M of sucrose solution was added to soils. Application of three linear transformations of the Michaelis-Menten equation indicated that the apparent K m constants varied among the soils studied, but the results obtained by the three plots were similar. By using the Lineweaver-Burk plot, the K m values in five soils ranged from 16.3 to 42.1 (avg.=24.5) m M and V max values ranged from 1.98 to 7.37 mg of reducing sugars released/g of soil/24 h. The optimum temperature for invertase activity in soils was observed at 50°C and denaturation of the enzyme began at 55°C.
Biochemical Calculations Segel Pdf
The activation energy (E a) and enthalpy of activation (ΔH.) values for invertase activity, expressed in kJ/mole, ranged from 6.1 to 43.1 and 3.5 to 40.5, respectively. The Q 10 values for the invertase reaction in soils with a temperature range to 10 to 50°C ranged from 1.08 to 1.96. Under standerd conditions, the accumulation of reducing sugars was linear with time up to 48 h. Among the various pretreatments that affected invertase activity in soils, toluene, TCA, and PMA inhibited the enzyme by an average of 19, 54, and 11%, respectively. Steam-sterilization essentially destroyed soil invertase.
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