Unveiling cofactor inhibition mechanisms in horse liver alcohol dehydrogenase: An allosteric driven regulation.

Horse Liver Alcohol Dehydrogenase (HLADH) is an extensively studied enzyme isolated from equine liver tissue, and holds a central role in numerous enzymatic processes, underscoring the need for thorough investigation. This study delves into the kinetic behavior and structural dynamics of HLADH, shedding light on complex mechanisms governing its catalytic activity and interactions with the cofactor. Notably, deviations from traditional Michaelis-Menten kinetics are observed, manifesting as a slowdown in catalytic rate under high NADH concentrations.

Prevention of Swelling Phenomenon of Alginate Beads To Improve the Stability and Recyclability of Encapsulated Horse Liver Alcohol Dehydrogenase.

Horse Liver Alcohol Dehydrogenase (HLADH) has been immobilized on calcium-alginate beads and used for both oxidation and reduction reactions. To avoid swelling of the beads and their subsequent breakage, calcium ions were added to both reaction and storage solutions, allowing the beads to maintain the initial structural features. The techniques used for this purpose revealed that 2 mM Ca is the optimal concentration, which does not significantly change the weight of the beads, the amount of water in them, and their external and internal structure.