Substrate-enzyme interactions in cellulase systems

Ida Lee, Barbara R. Evans, Lynette M. Lane, Jonathan Woodward

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The interaction between catalytically active and inactive Trichoderma reesei cellulase components and cotton fibers has been examined by scanning electron microscopy (SEM) and atomic force microscopy (AFM). Cellobiohydrolase I (CBH I), the major component, was rendered catalytically inactive by its treatment with ammonium hexachloropalladate; however, the inactive enzyme still had the ability to bind to the cotton fiber. SEM and AFM provided evidence suggesting that the catalytic activity of CBH I was required for fiber disruption AFM allowing resolution of cotton fibers to the microfibril level. However at high magnification slightly elongated holes were observed throughout the surface of the microfibrillar surface of cotton fibers treated with inactivated CBH I. No disruption of cotton fibers was observed by a palladium-inactivated CBH II/EG II mixture.

Original languageEnglish
Pages (from-to)163-169
Number of pages7
JournalBioresource Technology
Volume58
Issue number2
DOIs
StatePublished - Nov 1996

Funding

The authorst hank Mark Reevesf or reviewingt he manuscriptM, ary Jo Kreger for secretariasle rvices, and Marsha Savagef or editingt he manuscriptT.h is work was supportedb y the Division of Chemical Sciences, Office of Basic Energy Sciences, U.S. Departmenotf Energy,O ak Ridge NationalL abora-tory is managed by Lockheed Martin Energy Systems,In c., for the U.S. Departmenot f Energy underc ontracDt E-AC05-84OR21400.

FundersFunder number
Division of Chemical Sciences
U.S. Departmenot f EnergyE-AC05-84OR21400
U.S. Departmenotf Energy
Lockheed Martin
Basic Energy Sciences

    Keywords

    • Atomic force microscopy
    • Cellobiohydrolase I
    • Cellulase
    • Cotton fiber disruption
    • Palladium inactivation

    Fingerprint

    Dive into the research topics of 'Substrate-enzyme interactions in cellulase systems'. Together they form a unique fingerprint.

    Cite this