Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption

Jenni L. Rahikainen; Raquel Martin-Sampedro; Harri Heikkinen; Stella Rovio; Kaisa Marjamaa; Tarja Tamminen; Orlando J. Rojas; Kristiina Kruus

doi:10.1016/j.biortech.2013.01.075

Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption

Jenni L. Rahikainen^*, Raquel Martin-Sampedro, Harri Heikkinen, Stella Rovio, Kaisa Marjamaa, Tarja Tamminen, Orlando J. Rojas, Kristiina Kruus

^*Corresponding author for this work

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

355 Citations (Scopus)

Abstract

The effect of lignin as an inhibitory biopolymer for the enzymatic hydrolysis of lignocellulosic biomass was studied; specially addressing the role of lignin in non-productive enzyme adsorption. Botanical origin and biomass pre-treatment give rise to differences in lignin structure and the effect of these differences on enzyme binding and inhibition were elucidated. Lignin was isolated from steam explosion (SE) pre-treated and non-treated spruce and wheat straw and used for the preparation of ultrathin films for enzyme binding studies. Binding of Trichoderma reesei Cel7A (CBHI) and the corresponding Cel7A-core, lacking the linker and the cellulose-binding domain, to the lignin films was monitored using a quartz crystal microbalance (QCM). SE pre-treatment altered the lignin structure, leading to increased enzyme adsorption. Thus, the positive effect of SE pre-treatment, opening the cell wall matrix to make polysaccharides more accessible, may be compromised by the structural changes of lignin that increase non-productive enzyme adsorption. (C) 2013 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	270-278
Number of pages	9
Journal	Bioresource Technology
Volume	133
DOIs	https://doi.org/10.1016/j.biortech.2013.01.075
Publication status	Published - Apr 2013
MoE publication type	A1 Journal article-refereed

Funding

This work was enabled by funding from Graduate School for Biomass Refining (Academy of Finland), EU-projects DISCO (Grant Agreement No. 211863) and HYPE (Grant Agreement No. 213139) and FiDiPro LignoCell-project (Finnish Funding Agency for Technology and Innovation, Tekes and Academy of Finland). ROAL Oy (Terhi Puranen) is acknowledged for providing enzymes for this work. Jari Leino from VU, Espoo is acknowledged for performing the biomass pre-treatments. Juha Lagerbom and Mika Heikkinen from VTT, Tampere are acknowledged for the extensive the ball-milling effort. Prof. Stefan Willfor and Jens Krogell from Abo Akademi are acknowledged for providing facilities and help with the large-scale acetone extractions. Taina Ohra-aho and Leena-Sisko Johansson are acknowledged for performing the Py-GC/MS and XPS analysis, respectively. Dilek Ercili-Cura is acknowledged for taking the confocal microscopy image.

Keywords

Lignin
Steam explosion pre-treatment
Cellulase binding
Trichoderma reesei Cel7A
Carbohydrate binding module
STEAM-EXPLOSION PRETREATMENT
TRICHODERMA-REESEI
CELLOBIOHYDROLASE-I
WHEAT-STRAW
THIN-FILMS
HYDROLYSIS
WOOD
SOFTWOOD
SURFACE
DELIGNIFICATION

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10.1016/j.biortech.2013.01.075

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title = "Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption",

abstract = "The effect of lignin as an inhibitory biopolymer for the enzymatic hydrolysis of lignocellulosic biomass was studied; specially addressing the role of lignin in non-productive enzyme adsorption. Botanical origin and biomass pre-treatment give rise to differences in lignin structure and the effect of these differences on enzyme binding and inhibition were elucidated. Lignin was isolated from steam explosion (SE) pre-treated and non-treated spruce and wheat straw and used for the preparation of ultrathin films for enzyme binding studies. Binding of Trichoderma reesei Cel7A (CBHI) and the corresponding Cel7A-core, lacking the linker and the cellulose-binding domain, to the lignin films was monitored using a quartz crystal microbalance (QCM). SE pre-treatment altered the lignin structure, leading to increased enzyme adsorption. Thus, the positive effect of SE pre-treatment, opening the cell wall matrix to make polysaccharides more accessible, may be compromised by the structural changes of lignin that increase non-productive enzyme adsorption. (C) 2013 Elsevier Ltd. All rights reserved.",

keywords = "Lignin, Steam explosion pre-treatment, Cellulase binding, Trichoderma reesei Cel7A, Carbohydrate binding module, STEAM-EXPLOSION PRETREATMENT, TRICHODERMA-REESEI, CELLOBIOHYDROLASE-I, WHEAT-STRAW, THIN-FILMS, HYDROLYSIS, WOOD, SOFTWOOD, SURFACE, DELIGNIFICATION",

author = "Rahikainen, \{Jenni L.\} and Raquel Martin-Sampedro and Harri Heikkinen and Stella Rovio and Kaisa Marjamaa and Tarja Tamminen and Rojas, \{Orlando J.\} and Kristiina Kruus",

year = "2013",

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doi = "10.1016/j.biortech.2013.01.075",

language = "English",

volume = "133",

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journal = "Bioresource Technology",

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AU - Martin-Sampedro, Raquel

AU - Heikkinen, Harri

AU - Rovio, Stella

AU - Marjamaa, Kaisa

AU - Tamminen, Tarja

AU - Rojas, Orlando J.

AU - Kruus, Kristiina

PY - 2013/4

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N2 - The effect of lignin as an inhibitory biopolymer for the enzymatic hydrolysis of lignocellulosic biomass was studied; specially addressing the role of lignin in non-productive enzyme adsorption. Botanical origin and biomass pre-treatment give rise to differences in lignin structure and the effect of these differences on enzyme binding and inhibition were elucidated. Lignin was isolated from steam explosion (SE) pre-treated and non-treated spruce and wheat straw and used for the preparation of ultrathin films for enzyme binding studies. Binding of Trichoderma reesei Cel7A (CBHI) and the corresponding Cel7A-core, lacking the linker and the cellulose-binding domain, to the lignin films was monitored using a quartz crystal microbalance (QCM). SE pre-treatment altered the lignin structure, leading to increased enzyme adsorption. Thus, the positive effect of SE pre-treatment, opening the cell wall matrix to make polysaccharides more accessible, may be compromised by the structural changes of lignin that increase non-productive enzyme adsorption. (C) 2013 Elsevier Ltd. All rights reserved.

AB - The effect of lignin as an inhibitory biopolymer for the enzymatic hydrolysis of lignocellulosic biomass was studied; specially addressing the role of lignin in non-productive enzyme adsorption. Botanical origin and biomass pre-treatment give rise to differences in lignin structure and the effect of these differences on enzyme binding and inhibition were elucidated. Lignin was isolated from steam explosion (SE) pre-treated and non-treated spruce and wheat straw and used for the preparation of ultrathin films for enzyme binding studies. Binding of Trichoderma reesei Cel7A (CBHI) and the corresponding Cel7A-core, lacking the linker and the cellulose-binding domain, to the lignin films was monitored using a quartz crystal microbalance (QCM). SE pre-treatment altered the lignin structure, leading to increased enzyme adsorption. Thus, the positive effect of SE pre-treatment, opening the cell wall matrix to make polysaccharides more accessible, may be compromised by the structural changes of lignin that increase non-productive enzyme adsorption. (C) 2013 Elsevier Ltd. All rights reserved.

KW - Lignin

KW - Steam explosion pre-treatment

KW - Cellulase binding

KW - Trichoderma reesei Cel7A

KW - Carbohydrate binding module

KW - STEAM-EXPLOSION PRETREATMENT

KW - TRICHODERMA-REESEI

KW - CELLOBIOHYDROLASE-I

KW - WHEAT-STRAW

KW - THIN-FILMS

KW - HYDROLYSIS

KW - WOOD

KW - SOFTWOOD

KW - SURFACE

KW - DELIGNIFICATION

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U2 - 10.1016/j.biortech.2013.01.075

DO - 10.1016/j.biortech.2013.01.075

M3 - Article

SN - 0960-8524

VL - 133

SP - 270

EP - 278

JO - Bioresource Technology

JF - Bioresource Technology

ER -

Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption

Abstract

Funding

Keywords

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