Immobilization stabilizing additives

Colloidal Pt/RuO c- (C5 0.4nm) stabilized by a surfactant was prepared by co-hydrolysis of PtCU and RuCls under basic conditions. The Pt Ru ratio in the colloids can be between 1 4 and 4 1 by variation of the stoichiometry of the transition metal salts. The corresponding zerovalent metal colloids are obtained by the subsequent application of H2 to the colloidal Pt/Ru oxides (optionally in the immobilized form). Additional metals have been included in the metal oxide concept [Eq. (10)] in order to prepare binary and ternary mixed metal oxides in the colloidal form. Pt/Ru/WO c is regarded as a good precatalyst especially for the application in DMECs. Main-group elements such as A1 have been included in multimetallic alloy systems in order to improve the durability of fuel-cell catalysts. PtsAlCo.s alloyed with Cr, Mo, or W particles of 4—7-nm size has been prepared by sequential precipitation on conductant carbon supports such as highly disperse Vulcan XC72 [70]. Alternatively, colloidal precursors composed of Pt/Ru/Al allow... 

Due to tile conqilex nature of HS, it is conceivable that different parts of tiie HS structure may mediate different functions regarding metal ion mobilization or immobilization. In addition, different HS substructures have different biogeochemical turnover rates, mainly due to physical or chemical protection by soil matrix and/or innate biochemical stability. For exanqile, strongly bound... 

The discussion actually is focussing on the range between the two extremes. For the most favourable case, stabilizing additives affect permanent fixation of pollutants under realistic conditions which equals "immobilization". If dispersion of pollutants is significantly reduced, then the term "demobilization" would be appropriate. During stabilization or demobilization, different approaches can be taken, which also can be combined ... 

Enzymatic Reactors Adding free enzyme to a batch reactor is practical only when the value of the enzyme is relatively low. With expensive enzymes, reuse by retaining the enzyme with some type of support makes great economic sense. As some activity is usually lost in tethering the enzyme and the additional operations cost money, stabihty is very important. However, many enzymes are stabilized by immobilization thus, many reuses may be possible. 

A great savings in enzyme consumption can be achieved by immobilizing the enzyme in the reactor (Fig. 12). In addition to the smaller amount of enzyme required, immobilization often increases the stability of the enzyme. Several designs of immobiliz-ed-enzyme reactors (lERs) have been reported, with open-tubular and packed-bed being the most popular. Open-tubular reactors offer low dispersion but have a relatively small surface area for enzyme attachment. Packed-bed reactors provide extremely high surface areas and improved mass transport at the cost of more dispersion. 

A variety of approaches exist for stabilizing proteins, for example, chemical modification, immobilization, and site-directed mutagenesis [95,96], but these techniques are not within the scope of this chapter. The focus here will be on stabilization of proteins via formulation development. The principal formulation strategy is to stabilize the protein using clinically acceptable additives (excipients) or through the use of suitable pharmaceutical-processing technologies. 

It should be pointed out that the addition of substances, which could improve the biocompatibility of sol-gel processing and the functional characteristics of the silica matrix, is practiced rather widely. Polyethylene glycol) is one of such additives [110— 113]. Enzyme stabilization was favored by formation of polyelectrolyte complexes with polymers. For example, an increase in the lactate oxidase and glycolate oxidase activity and lifetime took place when they were combined with poly(N-vinylimida-zole) and poly(ethyleneimine), respectively, prior to their immobilization [87,114]. To improve the functional efficiency of entrapped horseradish peroxidase, a graft copolymer of polyvinylimidazole and polyvinylpyridine was added [115,116]. As shown in Refs. [117,118], the denaturation of calcium-binding proteins, cod III parvalbumin and oncomodulin, in the course of sol-gel processing could be decreased by complexation with calcium cations. 

These examples demonstrate that additives can have a beneficial effect on the entrapped biopolymers. Unfortunately, they are generally not universal. The additives need to be found for individual immobilized biopolymers and that is not so easy to do. For instance, lactate oxidase retained its activity in a silica matrix if the enzyme was taken as a complex with poly(N-vinylimidazole) prior to the immobilization, but the polymer did not stabilize glycolate oxidase [87,114], Its stabilization was observed after an exchange of poly(N-vinylimidazole) for poly(ethyleneimine). This is a decisive disadvantage of the approaches because they do not offer a general solution that might be extended to any immobilized biopolymer. 

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