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    Interactions of Endoglucanases with Amorphous Cellulose Films Resolved by Neutron Reflectometry and Quartz Crystal Microbalance with Dissipation Monitoring

    Year: 2012

    Journal: Langmuir, 2012, 28 (22), pp 8348–8358, 20120618

    Authors: Gang Cheng†‡, Supratim Datta†, Zelin Liu§, Chao Wang§, Jaclyn K. Murton‡, Page A. Brown‡, Michael S. Jablin , Manish Dubey , Jaroslaw Majewski , Candice E. Halbert , James F. Browning , Alan R. Esker§, Brian J. Watson#, Haito Zhang#, Steven W. Hutcheson#, Dale L. Huber‡ , Kenneth L. Sale†‡, Blake A. Simmons†‡, and Michael S. Kent*†‡

    Last authors: Michael S. Kent

    Organizations: † Joint BioEnergy Institute, Emeryville, California, United States ‡ Sandia National Laboratories, Livermore, California and Albuquerque, New Mexico, United States § Department of Chemistry, Virginia Tech, Blacksburg, Virginia, United States Lujan Neutron Science Center, Los Alamos National Laboratories, Los Alamos, New Mexico, United States Spallation Neutron Source, Oak Ridge National Laboratory, Oak Ridge, Tennessee, United States # Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, United States Center for Integrated Nanotechnologies, Albuquerque, New Mexico, United States

    Country: USA, US, United States, United States of America, America

    A study of the interaction of four endoglucanases with amorphous cellulose films by neutron reflectometry (NR) and quartz crystal microbalance with dissipation monitoring (QCM-D) is reported. The endoglucanases include a mesophilic fungal endoglucanase (Cel45A from H. insolens), a processive endoglucanase from a marine bacterium (Cel5H from S. degradans), and two from thermophilic bacteria (Cel9A from A. acidocaldarius and Cel5A from T. maritima). The use of amorphous cellulose is motivated by the promise of ionic liquid pretreatment as a second generation technology that disrupts the native crystalline structure of cellulose. The endoglucanases displayed highly diverse behavior. Cel45A and Cel5H, which possess carbohydrate-binding modules (CBMs), penetrated and digested within the bulk of the films to a far greater extent than Cel9A and Cel5A, which lack CBMs. While both Cel45A and Cel5H were active within the bulk of the films, striking differences were observed. With Cel45A, substantial film expansion and interfacial broadening were observed, whereas for Cel5H the film thickness decreased with little interfacial broadening. These results are consistent with Cel45A digesting within the interior of cellulose chains as a classic endoglucanase, and Cel5H digesting predominantly at chain ends consistent with its designation as a processive endoglucanase.