Physical constraints and functional plasticity of cellulases

Autor: 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

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)

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

Externí odkaz: https://doaj.org/article/57fe6ad3515b457c841b93644728432e

Activity of fungal β-glucosidases on cellulose

Autor: Malene B. Keller, Trine H. Sørensen, Kristian B. R. M. Krogh, Mark Wogulis, Kim Borch, Peter Westh

Publikováno v: Biotechnology for Biofuels, Vol 13, Iss 1, Pp 1-7 (2020)

Abstract Background Fungal beta-glucosidases (BGs) from glucoside hydrolase family 3 (GH3) are industrially important enzymes, which convert cellooligosaccharides into glucose; the end product of the cellulolytic process. They are highly active again

Externí odkaz: https://doaj.org/article/6f3936f0693243aabca124660c683142

Rate Response of Poly(Ethylene Terephthalate)‐Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase

Autor: Thore B. Thomsen, Sune Schubert, Cameron J. Hunt, Kim Borch, Kenneth Jensen, Jesper Brask, Peter Westh, Anne S. Meyer

Publikováno v: Thomsen, T B, Schubert, S, Hunt, C J, Borch, K, Jensen, K, Brask, J, Westh, P & Meyer, A S 2023, ' Rate Response of Poly(Ethylene Terephthalate) (PET)-Hydrolases to Substrate Crystallinity: Basis for Understanding the Lag Phase ', ChemSusChem, vol. 16, no. 13, e202300291 . https://doi.org/10.1002/cssc.202300291

The rate response of PET-hydrolases to increased substrate crystallinity (XC) of poly(ethylene terephthalate) (PET) manifests as a rate-lowering effect that varies significantly for different enzymes. Herein, we report the influence of XC on the prod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f93762b53abb55bb86efbf106ed2f57
https://doi.org/10.1002/cssc.202300291

Sabatier Principle for Rationalizing Enzymatic Hydrolysis of a Synthetic Polyester

Autor: Jenny Arnling Bååth, Kenneth Jensen, Kim Borch, Peter Westh, Jeppe Kari

Publikováno v: Arnling Bååth, J, Jensen, K, Borch, K, Westh, P & Kari, J 2022, ' Sabatier Principle for Rationalizing Enzymatic Hydrolysis of a Synthetic Polyester ', JACS Au, vol. 2, no. 5, pp. 1223-1231 . https://doi.org/10.1021/jacsau.2c00204

Interfacial enzyme reactions are common in nature and in industrial settings, including the enzymatic deconstruction of poly(ethylene terephthalate) (PET) waste. Kinetic descriptions of PET hydrolases are necessary for both comparative analyses, disc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ecdc1a2418ef28af66fe5efb56f15c7
https://pubmed.ncbi.nlm.nih.gov/35647598

A steady-state approach for inhibition of heterogeneous enzyme reactions

Autor: Silke Flindt Badino, Peter Westh, Jeppe Kari, Kim Borch, Trine Holst Sørensen, Ana Mafalda Cavaleiro, Stine Fredslund Hansen, Corinna Schiano-di-Cola

Publikováno v: Biochemical Journal. 477:1971-1982

The kinetic theory of enzymes that modify insoluble substrates is still underdeveloped, despite the prevalence of this type of reaction both in vivo and industrial applications. Here, we present a steady-state kinetic approach to investigate inhibiti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6330a4a61d9fc11e74a406b6edec6ab
https://doi.org/10.1042/bcj20200083