Fungal Cellulases

被引:607
作者
Payne, Christina M. [1 ,2 ]
Knott, Brandon C. [3 ]
Mayes, Heather B. [4 ]
Hansson, Henrik [6 ]
Himmel, Michael E. [5 ]
Sandgren, Mats [6 ]
Stahlberg, Jerry [6 ]
Beckham, Gregg T. [3 ]
机构
[1] Univ Kentucky, Dept Chem & Mat Engn, Lexington, KY 40506 USA
[2] Univ Kentucky, Ctr Computat Sci, Lexington, KY 40506 USA
[3] Natl Renewable Energy Lab, Natl Bioenergy Ctr, Golden, CO 80401 USA
[4] Northwestern Univ, Dept Chem & Biol Engn, Evanston, IL 60208 USA
[5] Natl Renewable Energy Lab, Biosci Ctr, Golden, CO 80401 USA
[6] Swedish Univ Agr Sci, Uppsala BioCtr, Dept Chem & Biotechnol, SE-75651 Uppsala, Sweden
关键词
TRICHODERMA-REESEI CELLOBIOHYDROLASE; GLYCOSIDE HYDROLASE FAMILY; CELLULOSE-BINDING DOMAIN; X-RAY-SCATTERING; HEN EGG-WHITE; LYTIC POLYSACCHARIDE MONOOXYGENASE; HYDROGEN-BONDING SYSTEM; FLAVOCYTOCHROME CELLOBIOSE DEHYDROGENASE; ENCODING THERMOSTABLE CELLOBIOHYDROLASE; INTRINSICALLY UNSTRUCTURED PROTEINS;
D O I
10.1021/cr500351c
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The enzymatic hydrolysis step represents the second portion of biomass depolymerization and is a major cost driver in bioethanol production due to the high cost of enzyme production. Significant efforts have been expended to understand and improve natural paradigms for enzymatic depolymerization of biomass with the aim to decrease the cost of sugar production for fuels and chemicals production. Cellulase enzyme research has been accelerated due to renewed interest in the production of ethanol from lignocellulosic biomass. Third-generation biofuels are now undergoing focused research and development with the goal of cost-effective production of infrastructure-compatible fuels from lignocellulosic biomass including fuels to fulfill demands in the gasoline, diesel, jet fuel, and maritime sectors.
引用
收藏
页码:1308 / 1448
页数:141
相关论文
共 1052 条
[1]   NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions [J].
Aachmann, Finn L. ;
Sorlie, Morten ;
Skjak-Braek, Gudmund ;
Eijsink, Vincent G. H. ;
Vaaje-Kolstad, Gustav .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (46) :18779-18784
[2]   Dioxygen activation at a single copper site:: Structure, bonding, and mechanism of formation of 1:1 Cu-O2 adducts [J].
Aboelella, NW ;
Kryatov, SV ;
Gherman, BF ;
Brennessel, WW ;
Young, VG ;
Sarangi, R ;
Rybak-Akimova, EV ;
Hodgson, KO ;
Hedman, B ;
Solomon, EI ;
Cramer, CJ ;
Tolman, WB .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (51) :16896-16911
[3]  
ABUJA PM, 1988, EUR BIOPHYS J BIOPHY, V15, P339, DOI 10.1007/BF00254721
[4]   DOMAIN-STRUCTURE OF CELLOBIOHYDROLASE-II AS STUDIED BY SMALL-ANGLE X-RAY-SCATTERING - CLOSE RESEMBLANCE TO CELLOBIOHYDROLASE-I [J].
ABUJA, PM ;
PILZ, I ;
CLAEYSSENS, M ;
TOMME, P .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 156 (01) :180-185
[5]   STRUCTURAL-CHANGES IN CELLOBIOHYDROLASE I UPON BINDING OF A MACROMOLECULAR LIGAND AS EVIDENT BY SAXS INVESTIGATIONS [J].
ABUJA, PM ;
PILZ, I ;
TOMME, P ;
CLAEYSSENS, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 165 (02) :615-623
[6]   Technoeconomic analysis of the dilute sulfuric acid and enzymatic hydrolysis process for the conversion of corn stover to ethanol [J].
Aden, Andy ;
Foust, Thomas .
CELLULOSE, 2009, 16 (04) :535-545
[7]   Probing the role of N-linked glycans in the stability and activity of fungal cellobiohydrolases by mutational analysis [J].
Adney, William S. ;
Jeoh, Tina ;
Beckham, Gregg T. ;
Chou, Yat-Chen ;
Baker, John O. ;
Michener, William ;
Brunecky, Roman ;
Himmel, Michael E. .
CELLULOSE, 2009, 16 (04) :699-709
[8]   Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation [J].
Agger, Jane W. ;
Isaksen, Trine ;
Varnai, Aniko ;
Vidal-Melgosa, Silvia ;
Willats, William G. T. ;
Ludwig, Roland ;
Horn, Svein J. ;
Eijsink, Vincent G. H. ;
Westereng, Bjorge .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (17) :6287-6292
[9]   Positional expression effects of cysteine mutations in the Thermobifida fusca cellulase Cel6A and Cel6B catalytic domains [J].
Ai, YC ;
Zhang, S ;
Wilson, DB .
ENZYME AND MICROBIAL TECHNOLOGY, 2003, 32 (02) :331-336
[10]   Mutation and expression of N233C-D506C of cellulase Cel6B from Thermobifida fusca in Escherichia coli [J].
Ai, YC ;
Wilson, DB .
ENZYME AND MICROBIAL TECHNOLOGY, 2002, 30 (06) :804-808