Cells enhanced catalytic stability

The most suitable driving force in BI is the reduction of the diffusion path that already operates in transport processes across biological bilayers. Consequently, biocatalyst membranes and specially designed bioreactors, such as jet loop and membrane reactors, are available to intensify biochemical reactions. " " Supported biocatalysts are often employed to enhance catalytic activity and stability and to protect enzymes/ microorganisms from mechanical degradation and deactivation.f Immobilization of the cells is one of the techniques employed to improve the productivity of bioreactors. 

In this review, we briefly discuss the dissolution and solubility of platinum (Sect. 2), the degradation of platinum nanoparticles in fuel cells (Sect. 3), and carbon corrosion (Sect. 4). We then describe new cathode electrocatalysts wherein the platinum content can be dramatically reduced, while offering possibiUties for enhancing catalytic activity and stability (Sect. 5). 

For Cl2 or 02 evolution the stability of ruthenium based electrodes is not sufficient on a technical scale. Therefore the possibility of stabilizing the ruthenium oxide without losing too much of its outstanding catalytic performance was investigated by many groups. For the Cl2 process, mixed oxides with valve metals like Ti or Ta were found to exhibit enhanced stability (see Section 3.1), while in the case of the 02 evolution process in solid polymer electrolyte cells for H2 production a mixed Ru/Ir oxide proved to be the best candidate [68, 80]. 

For each BoNT serotype, the dichain form constimtes the active configuration of the neurotoxin the isolated LC and HC are devoid of systemic toxicity. The absence of toxicity is consistent with findings that the LC cannot gain access to the cytosol unless it is coupled to the HC and that the HC lacks the ability to inhibit neurotransmitter release (Stecher et al., 1989 Goodnough et al., 2002). The isolated LC does, however, remain enzymatically active as evidenced by its ability to inhibit exocytosis from permeabilized chromaffin cells (Stecher et al., 1989), by its ability to cleave SNARE proteins in cell-free assays (Adler et al., 1998), and by its capacity to inhibit ACh release in skeletal muscle when delivered by liposomes (de Paiva and Dolly, 1990). It is not clear whether any portion of the HC is translocated along with the LC, and if so, whether it exerts a role in enhancing the catalytic activity or stability of the LC. 

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