Preferential adsorption and activity of monocomponent cellulases on lignocellulose thin films with varying lignin content

R. Martin-Sampedro (Corresponding Author), Jenni Rahikainen, L.-S. Johansson, Kaisa Marjamaa, J. Laine, Kristiina Kruus, O.J. Rojas (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

54 Citations (Scopus)

Abstract

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 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.
Original languageEnglish
Pages (from-to)1231-1239
Number of pages9
JournalBiomacromolecules
Volume14
Issue number4
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

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Cellulases
Lignin
Cellulose
Adsorption
Thin films
Quartz
Substrates
Crystal resonators
Enzymatic hydrolysis
lignocellulose
Hydrolysis
Biomass
Crystals

Cite this

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title = "Preferential adsorption and activity of monocomponent cellulases on lignocellulose thin films with varying lignin content",
abstract = "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 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.",
author = "R. Martin-Sampedro and Jenni Rahikainen and L.-S. Johansson and Kaisa Marjamaa and J. Laine and Kristiina Kruus and O.J. Rojas",
year = "2013",
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Preferential adsorption and activity of monocomponent cellulases on lignocellulose thin films with varying lignin content. / Martin-Sampedro, R. (Corresponding Author); Rahikainen, Jenni; Johansson, L.-S.; Marjamaa, Kaisa; Laine, J.; Kruus, Kristiina; Rojas, O.J. (Corresponding Author).

In: Biomacromolecules, Vol. 14, No. 4, 2013, p. 1231-1239.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Preferential adsorption and activity of monocomponent cellulases on lignocellulose thin films with varying lignin content

AU - Martin-Sampedro, R.

AU - Rahikainen, Jenni

AU - Johansson, L.-S.

AU - Marjamaa, Kaisa

AU - Laine, J.

AU - Kruus, Kristiina

AU - Rojas, O.J.

PY - 2013

Y1 - 2013

N2 - 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 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.

AB - 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 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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