Physical constrains and functional plasticity of cellulases: Linear scaling relationships for a heterogeneous enzyme reaction
Kari, J.; Molina, G.; Schaller, K.; Christensen, S.; Schiano-di-Cola, C.; Badino, S.; Soerensen, T.; Roejel, N.; Keller, M.; Kolaczkowski, B.; Olsen, J. P.; Krogh, K.; Jensen, K.; Cavaleiro, A. M.; Peters, G. H.; Spodsberg, N.; Borch, K.; Westh, P.
Show abstract
Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions of interfacial enzyme catalysis remain sparse, and this is partly due to a shortage of coherent experimental data to guide and assess such work. We have produced and kinetically characterized 83 cellulases, which revealed a conspicuous linear free energy relationship (LFER) between the strength of substrate binding and the activation barrier. This common scaling occurred despite the investigated enzymes were structurally and mechanistically diverse. We suggest that the scaling reflects basic physical restrictions of the hydrolytic process and that evolutionary selection have condensed cellulase phenotypes near the line. One consequence of the LFER is that the activity of a cellulase can be estimated from substrate binding strength, irrespectively of structural and mechanistic details, and this appears promising for in silico selection and design within this industrially important group of enzymes. On a more general note, the LFER may identify a link to inorganic heterogeneous catalysis, and hence open for the implementation of approaches from this field within interfacial enzymology.
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