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Preferential Adsorption and Activity of Monocomponent Cellulases on Lignocellulose Thin Films with Varying Lignin Content
journal contribution
posted on 2013-04-08, 00:00 authored by Raquel Martín-Sampedro, Jenni L. Rahikainen, Leena-Sisko Johansson, Kaisa Marjamaa, Janne Laine, Kristiina Kruus, Orlando J. RojasUnderstanding the enzymatic hydrolysis
of cellulose and the influence
of lignin in the process are critical for viable production of fuels
and chemicals from lignocellulosic biomass. The interactions of monocomponent
cellulases with cellulose and lignin substrates were investigated
by using thin films supported on quartz crystal microgravimetry (QCM)
resonators. Trichoderma reesei exoglucanase
(CBH-I) and endoglucanase (EG-I) bound strongly to both cellulose
and lignin but EG-I exhibited a distinctive higher affinity with lignin,
causing a more extensive inhibition of the cellulolytic reactions.
CBH-I was found to penetrate into the bulk of the cellulose substrate
increasing the extent of hydrolysis and film deconstruction. In the
absence of a cellulose binding domain (CBD) and a linker, the CBH-I
core adsorbed slowly and was not able to penetrate into the film.
Conversely to CBH-I, EG-I exhibited activity only on the surface of
the lignocellulose substrate even when containing a CBD and a linker.
Interestingly, EG-I displayed a clearly different interaction profile
as a function of contact time registered by QCM.
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Keywords
contact timeVarying Lignin ContentUnderstandingPreferential AdsorptionMonocomponent CellulasesTrichoderma reesei exoglucanaselinkerQCMfilm deconstructionlignocellulosic biomassquartz crystal microgravimetrymonocomponent cellulasescellulose substrateinteraction profilelignin substratesCBDlignocellulose substratecellulose binding domainhydrolysiscellulolytic reactions
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