Loop engineering in the thermophile cellobiohydrolase, Cel7A from Rasamsonia emersonii: Effects on activity and substrate interactions

Authors

  • Trine Holst S?rensen

Abstract

Cel7A cellobiohydrolases perform processive hydrolysis on one strand of cellulose, which is threaded through the enzyme?s substrate binding tunnel. The tunnel structure results from a groove in the catalytic domain, which is covered by a number of loops. These loops have been identified as potential targets for engineering of this industrially important enzyme family, but only few systematic studies on this have been made. In the current work we study two Asn residues in the B2 loop of the thermostable Cel7A from Rasamsonia emersonii. We found that Asn194 and particularly Asn197 promoted substrate binding, and the replacement of one or both of these. Forfattere: Trine Holst S?rensen, Michael S. Windahl, Jeppe Kari, Johan Olsen Kim Borch & Peter Westh (manuscript in preparation) DENNE ARTIKEL ER P? GRUND AF OPHAVSRETSM?SSIGE ?RSAGER DESV?RRE IKKE TILG?NGELIG Kontakt evt. forfatterne for at f? en kopi af artiklen. DUE TO THE LICENSE AGREEMENT WITH THE PUBLISHER, THIS ARTICLE IS NOT AVAILABLE Contact the authors for a copy of the article.

Published

2016-01-01

Issue

Kinetic and thermodynamic description of Cel7A catalyzed hydrolysis of cellulose, nr. 2, 2016

Section

Articles

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