RESUMEN
It was shown experimentally that the increase in the adsorption ability of cellulases leads to a sharp increase of the rate of the enzymatic degradation of crystalline cellulose. At the same time the rate of degradation of amorphous cellulose does not depend on the adsorption ability of cellulases. These effects have been explained using a model which takes into consideration the influence of the structure of the solid substrate on the surface mobility of the adsorbed molecules of the enzyme. The equations were derived which inter-relate the catalytic and the adsorptive properties of cellulases.
Asunto(s)
Celulasa/metabolismo , Celulosa/metabolismo , Adsorción , Cinética , Matemática , Modelos Biológicos , Unión Proteica , TermodinámicaRESUMEN
The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.