Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics

Miriam Kellock; Jenni Rahikainen; Kaisa Marjamaa; Kristiina Kruus

doi:10.1016/j.biortech.2017.01.072

Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics

Miriam Kellock, Jenni Rahikainen, Kaisa Marjamaa, Kristiina Kruus (Corresponding Author)

Research output: Contribution to journal › Article › Scientific › peer-review

26 Citations (Scopus)

Abstract

Non-productive enzyme binding onto lignin is the major inhibitory mechanism, which reduces hydrolysis rates and yields and prevents efficient enzyme recycling in the hydrolysis of lignocellulosics. The detailed mechanisms of binding are still poorly understood. Enzyme-lignin interactions were investigated by comparing the structural properties and binding behaviour of fungal monocomponent enzymes, cellobiohydrolases TrCel7A and TrCel6A, endoglucanases TrCel7B and TrCel5A, a xylanase TrXyn11 and a ß-glucosidase AnCel3A, onto lignins isolated from steam pretreated spruce and wheat straw. The enzymes exhibited decreasing affinity onto lignin model films in the following order: TrCel7B > TrCel6A > TrCel5A > AnCel3A > TrCel7A > TrXyn11. As analysed in Avicel hydrolysis, TrCel6A and TrCel7B were most inhibited by lignin isolated from pretreated spruce. This could be partially explained by adsorption of the enzyme onto the lignin surface. Enzyme properties, such as enzyme surface charge, thermal stability or surface hydrophobicity could not alone explain the adsorption behaviour.

Original language	English
Pages (from-to)	183-191
Number of pages	9
Journal	Bioresource Technology
Volume	232
DOIs	https://doi.org/10.1016/j.biortech.2017.01.072
Publication status	Published - 11 Feb 2017
MoE publication type	A1 Journal article-refereed

Fingerprint

Cellulases

Lignin

lignin

hydrolysis

Hydrolysis

Enzymes

enzyme

Cellulose 1,4-beta-Cellobiosidase

Glucosidases

adsorption

Adsorption

Cellulase

Steam

Straw

hydrophobicity

Surface charge

Hydrophobicity

Cellulose

straw

Recycling

Keywords

lignin
non-productive binding
enzymatic hydrolysis
cellulase
xylanase

Cite this

Kellock, M., Rahikainen, J., Marjamaa, K., & Kruus, K. (2017). Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics. Bioresource Technology, 232, 183-191. https://doi.org/10.1016/j.biortech.2017.01.072

Kellock, Miriam ; Rahikainen, Jenni ; Marjamaa, Kaisa ; Kruus, Kristiina. / Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics. In: Bioresource Technology. 2017 ; Vol. 232. pp. 183-191.

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title = "Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics",

abstract = "Non-productive enzyme binding onto lignin is the major inhibitory mechanism, which reduces hydrolysis rates and yields and prevents efficient enzyme recycling in the hydrolysis of lignocellulosics. The detailed mechanisms of binding are still poorly understood. Enzyme-lignin interactions were investigated by comparing the structural properties and binding behaviour of fungal monocomponent enzymes, cellobiohydrolases TrCel7A and TrCel6A, endoglucanases TrCel7B and TrCel5A, a xylanase TrXyn11 and a {\ss}-glucosidase AnCel3A, onto lignins isolated from steam pretreated spruce and wheat straw. The enzymes exhibited decreasing affinity onto lignin model films in the following order: TrCel7B > TrCel6A > TrCel5A > AnCel3A > TrCel7A > TrXyn11. As analysed in Avicel hydrolysis, TrCel6A and TrCel7B were most inhibited by lignin isolated from pretreated spruce. This could be partially explained by adsorption of the enzyme onto the lignin surface. Enzyme properties, such as enzyme surface charge, thermal stability or surface hydrophobicity could not alone explain the adsorption behaviour.",

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Kellock, M, Rahikainen, J , Marjamaa, K & Kruus, K 2017, 'Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics', Bioresource Technology, vol. 232, pp. 183-191. https://doi.org/10.1016/j.biortech.2017.01.072

Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics. / Kellock, Miriam; Rahikainen, Jenni ; Marjamaa, Kaisa ; Kruus, Kristiina (Corresponding Author).

In: Bioresource Technology, Vol. 232, 11.02.2017, p. 183-191.

Research output: Contribution to journal › Article › Scientific › peer-review

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