Enzymatic biofuel cells and bioelectrochemical sensors are often limited in performance because of their inability to utilize all of the energy confined in chemical bonds of complex molecules. Multi-enzyme cascade catalysis provides a means to remedy this limitation, but efficiencies of such electrodes can be further enhanced by improving interenzyme substrate mass transport. This consideration is demonstrated to be advantageous in biological systems, as displayed by nearly ubiquitous organization of sequential enzymes in natural metabolic pathways. This sequential organization, termed a metabolon, is examined in this work for a two-enzyme pentose phosphate pathway bioelectrode for the oxidation of glucose. This two-enzyme electrode is compared with a single enzyme, glucose dehydrogenase, and demonstrates increased performance. In addition, increases in efficiency are demonstrated through the creation of a synthetic two-enzyme metabolon versus randomly suspended enzymes immobilized within a hydrogel matrix.
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Moehlenbrock et al. (2011) studied this question.
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