Engineering of Class II Cellobiose Dehydrogenases for Improved Glucose Sensitivity and Reduced Maltose Affinity. Issue 4 (16th March 2017)

• Record Type: Journal Article
• Authors: Ortiz, Roberto; Rahman, Mahbubur; Zangrilli, Beatrice; Sygmund, Christoph; Micheelsen, Pernille O.; Silow, Maria; Toscano, Miguel D.; Ludwig, Roland; Gorton, Lo
• Is Part Of: ChemElectroChem. Volume 4:Issue 4(2017)
• Page Start: 750
• Page End: 750
• Publication Date: 2017-03-16
• Subjects: Electrochemistry -- Periodicals; 541.37
• DOI: 10.1002/celc.201700226
• Languages: English
• ISSNs: 2196-0216

Abstract

Abstract: The front cover artwork is provided by Prof. Lo Gorton from Lund University (Sweden) and his co‐workers. The image shows mutated cellobiose dehydrogenase (CDH) immobilized on a graphite electrode and how preferentially glucose is oxidized by this enzyme. Read the full text of the Article at 10.1002/celc.201600781 . Abstract : "A single mutation from CYS to TYR on the active site of the enzymes Ct CDH and Hi CDH produces a remarkable increase in the activity and affinity for glucose as well as a decrease for maltose. The presented work combined with the low potential values inherent to cellobiose dehydrogenase (CDH) shows a new methodology to improve the usage of Class II CDHs towards mediatorless glucose biosensors and biofuel cells…" Find out more about the story behind the front cover research at10.1002/celc.201600781 .