Article

Abstract

• The conversion of biomass into green fuels and chemicals is of great societal interest. Engineers have been designing new cellulase enzymes for the breakdown of otherwise insoluble cellulose materials. A barrier to the rational design of new enzymes has been our lack of a molecular picture of how cellulase binding occurs. A critical factor is the attachment via the enzyme’s carbohydrate binding module (CBM). To elucidate the structural and mechanistic details of cellulase adsorption, we have combined experimental data from sum frequency generation spectroscopy with molecular dynamics simulations to probe the equilibrium structure and surface alignment of a 14-residue peptide mimicking the CBM. The data show that binding is driven by hydrogen bonding and that tyrosine side chains within the CBM align the cellulase with the registry of the cellulose surface. Such an alignment is favorable for the translocation and effective cellulose breakdown and is therefore likely an important parameter for the design of novel enzymes.

   

Creator

• Mauri, Sergio
• Roeters, Steven J
• Pfaendtner, Jim
• Nishiyama, Yoshiharu
• Mertig, Rolf
• Sprenger, Kayla
• Weidner, Tobias

Academic Affiliation

• Chemical and Biological Engineering

Journal Title

• The Journal of Physical Chemistry Letters

Journal Issue/Number

• 43

Journal Volume

• 12

Last Modified

• 2023-07-10

Resource Type

• Article

Rights Statement

• In Copyright

DOI

•  https://doi.org/10.1021/acs.jpclett.1c02757

ISSN

• 1948-7185

Language

• English [eng]

Relationships

Items

Thumbnail	Title	Date Uploaded	Visibility	Actions
	manuscript_Sprenger_etal_R2.pdf	2023-07-10	Public	Download