Interfacial deactivation

Various enzymes have been reported to be susceptible to deactivation upon shearing due possibly to the disturbance of their tertiary structure. Several investigators have studied the interfacial deactivation of T. reesei enzymes (Kim et al., 1982 Reese and Mandels, 1980). The addition of a surfactant has been found to substantially reduce enzyme deactivation. The surfactant impedes the migration of enzyme to the air-liquid interface. 

First, in composites with high fiber concentrations, there is little matrix in the system that is not near a fiber surface. Inasmuch as polymerization processes are influenced by the diffusion of free radicals from initiators and from reactive sites, and because free radicals can be deactivated when they are intercepted at solid boundaries, the high interfacial area of a prepolymerized composite represents a radically different environment from a conventional bulk polymerization reactor, where solid boundaries are few and very distant from the regions in which most of the polymerization takes place. The polymer molecular weight distribution and cross-link density produced under such diffusion-controlled conditions will differ appreciably from those in bulk polymerizations. 

In the mechanism of an interfacial catalysis, the structure and reactivity of the interfacial complex is very important, as well as those of the ligand itself. Recently, a powerful technique to measure the dynamic property of the interfacial complex was developed time resolved total reflection fluorometry. This technique was applied for the detection of the interfacial complex of Eu(lII), which was formed at the evanescent region of the interface when bathophenanthroline sulfate (bps) was added to the Eu(lII) with 2-thenoyl-trifuluoroacetone (Htta) extraction system [11]. The experimental observation of the double component luminescence decay profile showed the presence of dinuclear complex at the interface as illustrated in Scheme 5. The lifetime (31 /as) of the dinuclear complex was much shorter than the lifetime (98 /as) for an aqua-Eu(III) ion which has nine co-ordinating water molecules, because of a charge transfer deactivation. 

The liquid-liquid interface has been identified as the major factor responsible for papain deactivation in a biphasic system [66]. If the interfacial tension can be decreased to a small value using surfactant, the biocatalyst stability will be expected to increase. 

As stated, one of the fundamental problems encountered in the direct oxidation of hydrocarbon fuels in SOFCs is carbon deposition on the anode, which quickly deactivates the anode and degrades cell performance. The possible buildup of carbon can lead to failure of the fuel-cell operation. Applying excess steam or oxidant reagents to regenerate anode materials would incur significant cost to SOFC operation. The development of carbon tolerant anode materials was summarized very well in several previous reviews and are not repeated here [7-9], In this section, the focus will be on theoretical studies directed toward understanding the carbon deposition processes in the gas-surface interfacial reactions, which is critical to the... 

The effectiveness of the method is most probably based on the fact that alkyl hypochlorite is formed at the oil/water interface where the cosurfactant alcohol resides. The oxidation that follows takes place either inside or on the surface of oil droplet. The rate of the reaction can result from a large hydrocarbon/water contact area permitting interaction between oil-soluble sulfide with interfacial cosurfactant that served as an intermediary. An extension ofthis procedure to mustard deactivation has also been proposed [20b]. Such systems could be also applied to the degradation of several environmentally contaminating materials The formation of microemulsions, micelles and vesicles is promoted by unfavourable interactions at the end sections of simple bilayer membranes. There is no simple theory of solute-solvent interactions. However, the formation of... 

Immobilization has other advantages it can slow enzyme deactivation by inhibiting protease attack and minimizing shear, interfacial, temperature, or solvent denaturation. As for the scarcity of some potentially very useful enzymes, it may be only a temporary problem. The development of cloning techniques, and probably the very increase in demand will result in lower prices. One spectacular instance is sialyl aldolase (see Table I). Industrial production of this enzyme by the gene-cloned strain of Escherichia coli has been reported.1,2 Sialylaldolase is now available from Toyobo at a moderate price. 

However, Thomas and Dimnill (1979) studied the effect of shear on catalase and urease activities by using a coaxial cylindrical viscometer that was sealed to prevent any air-liquid contact. They found that there was no significant loss of enzyme activity due to shear force alone at shear rates up to 106 sec-1. They reasoned that the deactivation observed by Charm and Wong (1970) was the result of a combination of shear, air-liquid interface, and some other effects which are not fully understood. Charm and Wong did not seal their shear apparatus. This was further confirmed, as cellulase deactivation due to the interfacial effect combined with the shear effect was found to be far more severe and extensive than that due to the shear effect alone (Jones and Lee, 1988). 

Consequently, less enzyme reaches the interface, where it will deactivate by unfolding when subjected to surface tension forces. The cellulase deactivation due to this interfacial effect combined with the shear effect was found to be far more severe and extensive than that due to the shear effect alone (Kirn et al., 1982). 

The influence of internal and interfacial diffusion on catalyst deactivation by simultaneous sintering and poisoning is examined. The study focuses on the copper catalyst used in the water gas shift reaction ( WGSR). It is found that catalyst life increases when internal and external poison diffusional resistance increases. Temperature reduces the total average activity but this effect is partially neutralized by the diffusional effects undergone by the reactants inside the pellet. 

Lee outlines three different physical methods that are commonly utilized for enzyme immobilization. Enzymes can be adsorbed physically onto a surface-active adsorbent, and adsorption is the simplest and easiest method. They can also be entrapped within a cross-linked polymer matrix. Even though the enzyme is not chemically modified during such entrapment, the enzyme can become deactivated during gel formation and enzyme leakage can be problematic. The microencapsulation technique immobilizes the enzyme within semipermeable membrane microcapsules by interfacial polymerization. All of these methods for immobilization facilitate the reuse of high-value enzymes, but they can also introduce external and internal mass-transfer resistances that must be accounted for in design and economic considerations. 

Another approach used for deactivating part of the amine groups of polyethylenimine was to use a partial quaternization of polyethylenimine with ethyl iodide. The membranes formed were similar in properties to those made by the partial polyethylenimine neutralization. Still another type of amine polymer was prepared by free radical polymerization of a mixture of diallylamine hydrochloride, dimethyl diallyl ammonium chloride and sulfur dioxide. This polymer in the free base form for interfacial reaction had reactive secondary amine groups and non-reactive quaternary amine groups ... 

By studying a series of Rh/Ti02 catalysts of varying metal dispersion, we noticed that the deactivating effect of HTR for ethane hydrogenolysis could be better correlated with the extent of interfacial perimeter around the metal particle than with the extent of interfacial metal-support contact area. In addition, we found that the kinetics of deactivation followed a square root of time dependence, which is generally observed for diffu-... 

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