Kinetics of product inhibition in alcohol fermentation-temperature effect in the “sake” brewing

1969 ◽  
Vol 11 (6) ◽  
pp. 1285-1287 ◽  
Author(s):  
S. Aiba ◽  
M. Shoda ◽  
M. Nagatani
Keyword(s):  
Temperature Effect ◽  
Product Inhibition ◽  
Alcohol Fermentation ◽  
Fermentation Temperature ◽  
Kinetics Of

Kinetics of product inhibition in alcohol fermentation

1968 ◽  
Vol 10 (6) ◽  
pp. 845-864 ◽  
Author(s):  
S. Aiba ◽  
M. Shoda ◽  
M. Nagatani
Keyword(s):  
Product Inhibition ◽  
Alcohol Fermentation ◽  
Kinetics Of

Temperature Effect on the Two-Dimensional Phase Transition Kinetics of Adenine Adsorbed at the Hg Electrode/Aqueous Solution Interface

2003 ◽  
Vol 68 (8) ◽  
pp. 1407-1419 ◽  
Author(s):  
Claudio Fontanesi ◽  
Roberto Andreoli ◽  
Luca Benedetti ◽  
Roberto Giovanardi ◽  
Paolo Ferrarini
Keyword(s):  
Phase Transition ◽  
Aqueous Solution ◽  
Phase Change ◽  
Temperature Effect ◽  
Transition Rate ◽  
Effect Of Temperature ◽  
Two Dimensional ◽  
Solution Interface ◽  
Phase Transition Kinetics ◽  
Kinetics Of

The kinetics of the liquid-like → solid-like 2D phase transition of adenine adsorbed at the Hg/aqueous solution interface is studied. Attention is focused on the effect of temperature on the rate of phase change; an increase in temperature is found to cause a decrease of transition rate.

scholarly journals Kinetics of alcohol fermentation at high yeast levels

1979 ◽  
Vol 21 (8) ◽  
pp. 1477-1482 ◽  
Author(s):  
E. J. del Rosario ◽  
Kye Joon Lee ◽  
P. L. Rogers
Keyword(s):  
Alcohol Fermentation ◽  
Kinetics Of

Cut Orientation And Drying Temperature Effect On Drying And Rehydration Kinetics Of Yacon (Smallanthus Sonchifolius)

2021 ◽  
Author(s):  
Lester Gleyser De Los Santos Pazos ◽  
Danny Chávez Novoa ◽  
Alexander Vega Anticona ◽  
Guillermo Linares ◽  
Jesús Sánchez-González ◽  
...  
Keyword(s):  
Temperature Effect ◽  
Drying Temperature ◽  
Smallanthus Sonchifolius ◽  
Kinetics Of

scholarly journals The kinetic mechanism of the major form of ox kidney aldehyde reductase with d-glucuronic acid

1982 ◽  
Vol 205 (2) ◽  
pp. 381-388 ◽  
Author(s):  
Ann K. Daly ◽  
Timothy J. Mantle
Keyword(s):  
Glucuronic Acid ◽  
Alternative Pathway ◽  
Kinetic Mechanism ◽  
Product Inhibition ◽  
Aldehyde Reductase ◽  
Major Form ◽  
Mechanism Of Inhibition ◽  
Steady State Kinetics ◽  
Inhibition Studies ◽  
Kinetics Of

The steady-state kinetics of the major form of ox kidney aldehyde reductase with d-glucuronic acid have been determined at pH7. Initial rate and product inhibition studies performed in both directions are consistent with a Di-Iso Ordered Bi Bi mechanism. The mechanism of inhibition by sodium valproate and benzoic acid is shown to involve flux through an alternative pathway.

Phase-plane geometries in enzyme kinetics

1994 ◽  
Vol 72 (3) ◽  
pp. 800-812 ◽  
Author(s):  
Simon J. Fraser ◽  
Marc R. Roussel
Keyword(s):  
Steady State ◽  
Phase Plane ◽  
Competitive Inhibition ◽  
Three Dimensional ◽  
Product Inhibition ◽  
Slow Manifold ◽  
Dimensional System ◽  
Planar System ◽  
State Behaviour ◽  
Kinetics Of

The transient and steady-state behaviour of the reversible Michaelis–Menten mechanism [R] and Competitive Inhibition (CI) mechanism is studied by analysis in the phase plane. Usually, the kinetics of both mechanisms is simplified to give a modified Michaelis–Menten velocity expression; this applies to the CI mechanism with excess inhibitor and to mechanism [R] in the product inhibition limit. In this paper, [R] is treated exactly as a plane autonomous system of differential equations and its true (dynamical) steady state is described by a line-like slow manifold M. Initial velocity experiments for [R] no longer strictly correspond to the hyperbolic law (as in the irreversible Michaelis–Menten mechanism) and this leads to corrections to the standard integrated rate law. Using a new analysis, the slow dynamics of the CI mechanism is reduced from a three-dimensional system to a planar system. In this mechanism transient decay collapses the trajectory flow onto a two-dimensional "slow" surface Σ; motion on Σ can be treated exactly as projected dynamics in the plane. This projected flow may differ in important ways from that of two-step mechanisms, e.g., it may lack a proper steady state. The relevance of these more accurate dynamical descriptions is discussed in relation to experimental design and metabolic function.

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