Phenomenological kinetics of wood delignification: application of a time-dependent rate constant and a generalized severity parameter to pulping and correlation of pulp properties

1994 ◽  
Vol 28 (6) ◽  
Author(s):  
D. Montan� ◽  
J. Salvad� ◽  
X. Farriol ◽  
P. Jollez ◽  
E. Chornet
2021 ◽  
Vol 379 ◽  
pp. 321-334
Author(s):  
Kevin Cronin ◽  
Francisco J. Gutiérrez Ortiz ◽  
Denis Ring ◽  
Fuweng Zhang

1969 ◽  
Vol 47 (20) ◽  
pp. 3773-3778 ◽  
Author(s):  
M. L. Sanduja ◽  
W. MacF. Smith

The kinetics of formation of the monophenanthroline complex of nickel(II) has been studied spectrophotometrically in water–methanol mixtures of 0 to 97 weight % of methanol, at ionic strength 0.050, at varying acidities at 25 °C. Values for the rate constants for the acid independent and acid dependent reactions together with values for the equilibrium acid ionization quotient of phenanthrolium ion over the range of solvent mixtures have been determined. The values of the acid independent rate constant show little dependence on solvent compositions up to 76% methanol, then decrease and show no correlation with trends in the ionization quotient of phenanthrolium ion. The acid dependent rate constant shows only a modest dependence on solvent composition over most of the range of solvent compositions except in the range of highest methanol content where it is not significantly different from zero.


1979 ◽  
Vol 181 (3) ◽  
pp. 775-778 ◽  
Author(s):  
K Brocklehurst

To facilitate mechanistic interpretation of the kinetics of time-dependent inhibition of enzymes and of similar protein modification reactions, it is important to know when the equilibrium assumption may be applied to the model: formula: (see text). The conventional criterion of quasi-equilibrium, k + 2 less than k-1, is not always easy to assess, particularly when k + 2 cannot be separately determined. It is demonstrated that the condition k + 2 less than k-1 is necessarily true, however, when the value of the apparent second-order rate constant for the modification reaction is much smaller than the value of k + 1. Since k + 1 is commonly at least 10(7)M-1.S-1 for substrates, it is probable that the equilibrium assumption may be properly applied to most irreversible inhibitions and modification reactions.


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