Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate

被引:88
作者
Bernardes, A. [1 ]
Pellegrini, V. O. A. [1 ]
Curtolo, F. [1 ]
Camilo, C. M. [1 ]
Mello, B. L. [1 ]
Johns, M. A. [2 ,3 ,6 ]
Scott, J. L. [4 ,5 ]
Guimaraes, F. E. C. [1 ]
Polikarpov, I. [1 ]
机构
[1] Univ Sao Paulo, Sao Carlos Inst Phys, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP, Brazil
[2] Univ Bath, EPSRC Ctr Doctoral Training Sustainable Chem Tech, Bath BA2 7AY, Avon, England
[3] Univ Bath, Dept Chem Engn, Bath BA2 7AY, Avon, England
[4] Univ Bath, Ctr Sustainable Chem Technol, Bath BA2 7AY, Avon, England
[5] Univ Bath, Dept Chem, Bath BA2 7AY, Avon, England
[6] Univ Bristol, Dept Aerosp Engn, Queens Bldg, Bristol BS8 1TR, Avon, England
基金
巴西圣保罗研究基金会;
关键词
Carbohydrate binding modules; Lignocellulosic biomass; Cellulose hydrolysis; Cellulases; TRICHODERMA-REESEI; DOMAIN; CEL7A; ADSORPTION; ENDOGLUCANASE; REVERSIBILITY; BIOCHEMISTRY; TEMPERATURE; EFFICIENCY; MECHANISM;
D O I
10.1016/j.carbpol.2019.01.108
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Plant biomass is a low-cost and abundant source of carbohydrates for production of fuels, "green" chemicals and materials. Currently, biochemical conversion of the biomass into sugars via enzymatic hydrolysis is the most viable technology. Here, the role of carbohydrate binding modules (CBMs) in the disruption of insoluble polysaccharide structures and their capacity to enhance cellulase-promoted lignocellulosic biomass hydrolysis was investigated. We show that CBM addition promotes generation of additional reducing ends in the insoluble substrate by cellulases. On the contrary, bovine serum albumin (BSA), widely used in prevention of a nonspecific protein binding, causes an increase in soluble reducing-end production, when applied jointly with cellulases. We demonstrate that binding of CBMs to cellulose is non-homogeneous, irreversible and leads to its amorphisation. Our results also reveal effects of CBM-promoted amorphogenesis on cellulose hydrolysis by cellulases.
引用
收藏
页码:57 / 68
页数:12
相关论文
共 67 条
[61]   DOMAIN FUNCTION IN TRICHODERMA-REESEI CELLOBIOHYDROLASES [J].
TEERI, T ;
REINIKAINEN, T ;
RUOHONEN, L ;
JONES, TA ;
KNOWLES, JKC .
JOURNAL OF BIOTECHNOLOGY, 1992, 24 (02) :169-176
[62]   STUDIES OF THE CELLULOLYTIC SYSTEM OF TRICHODERMA-REESEI QM-9414 - ANALYSIS OF DOMAIN FUNCTION IN 2 CELLOBIOHYDROLASES BY LIMITED PROTEOLYSIS [J].
TOMME, P ;
VANTILBEURGH, H ;
PETTERSSON, G ;
VANDAMME, J ;
VANDEKERCKHOVE, J ;
KNOWLES, J ;
TEERI, T ;
CLAEYSSENS, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 170 (03) :575-581
[63]   Carbohydrate-Binding Modules of Fungal Cellulases: Occurrence in Nature, Function, and Relevance in Industrial Biomass Conversion [J].
Varnai, Aniko ;
Makela, Miia R. ;
Djajadi, Demi T. ;
Rahikainen, Jenni ;
Hatakka, Annele ;
Viikari, Liisa .
ADVANCES IN APPLIED MICROBIOLOGY, VOL 88, 2014, 88 :103-165
[64]   Synergism in binary mixtures of Thermobifida fusca cellulases Cel6B, Cel9A, and Cel5A on BMCC and Avicel [J].
Watson, DL ;
Wilson, DB ;
Walker, LP .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2002, 101 (02) :97-111
[65]   Cellulose-binding domain of endoglucanase III from Trichoderma reesei disrupting the structure of cellulose [J].
Xiao, ZZ ;
Gao, PJ ;
Qu, YB ;
Wang, TH .
BIOTECHNOLOGY LETTERS, 2001, 23 (09) :711-715
[66]   The I-TASSER Suite: protein structure and function prediction [J].
Yang, Jianyi ;
Yan, Renxiang ;
Roy, Ambrish ;
Xu, Dong ;
Poisson, Jonathan ;
Zhang, Yang .
NATURE METHODS, 2015, 12 (01) :7-8
[67]   Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems [J].
Zhang, YHP ;
Lynd, LR .
BIOTECHNOLOGY AND BIOENGINEERING, 2004, 88 (07) :797-824