4.7 Article

Preferential Adsorption and Activity of Monocomponent Cellulases on Lignocellulose Thin Films with Varying Lignin Content

Journal

BIOMACROMOLECULES
Volume 14, Issue 4, Pages 1231-1239

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/bm400230s

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Funding

  1. Academy of Finland
  2. Lignocel Project (TEKES, Finland)

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Understanding 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 microgravimetty (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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