Physical constraints and functional plasticity of cellulases

Physical constraints and functional plasticity of cellulases

Enzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a s...

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Autores principales: Jeppe Kari, Gustavo A. Molina, Kay S. Schaller, Corinna Schiano-di-Cola, Stefan J. Christensen, Silke F. Badino, Trine H. Sørensen, Nanna S. Røjel, Malene B. Keller, Nanna Rolsted Sørensen, Bartlomiej Kolaczkowski, Johan P. Olsen, Kristian B. R. M. Krogh, Kenneth Jensen, Ana M. Cavaleiro, Günther H. J. Peters, Nikolaj Spodsberg, Kim Borch, Peter Westh
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Science
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Acceso en línea:https://doaj.org/article/57fe6ad3515b457c841b93644728432e
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Sumario:Enzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a so-called linear free energy relationship, which may help rationalize cellulolytic mechanisms and guide the selection of technical enzymes.

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