Thermostable Enzymes as Biocatalysts in the Biofuel Industry

被引:213
|
作者
Yeoman, Carl J. [1 ,4 ]
Han, Yejun [1 ,2 ]
Dodd, Dylan [1 ,2 ,3 ]
Schroeder, Charles M. [1 ,2 ,5 ,6 ]
Mackie, Roderick I. [1 ,2 ,4 ]
Cann, Isaac K. O. [1 ,2 ,3 ,4 ]
机构
[1] Univ Illinois, Inst Genom Biol, Urbana, IL 61801 USA
[2] Univ Illinois, Energy Biosci Inst, Urbana, IL 61801 USA
[3] Univ Illinois, Dept Microbiol, Urbana, IL 61801 USA
[4] Univ Illinois, Dept Anim Sci, Urbana, IL 61801 USA
[5] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA
[6] Univ Illinois, Dept Chem & Biomol Engn, Urbana, IL 61801 USA
关键词
ALPHA-L-ARABINOFURANOSIDASE; BACTERIUM THERMOTOGA-MARITIMA; BETA-D-XYLOSIDASE; STREPTOMYCES-THERMOVIOLACEUS OPC-520; CLOSTRIDIUM-THERMOCELLUM CELLULOSOME; THERMOPHILIC EUBACTERIUM THERMOTOGA; BACILLUS-THERMODENITRIFICANS TS-3; ARCHAEON SULFOLOBUS-SOLFATARICUS; THERMUS-NONPROTEOLYTICUS HG102; PROCESSIVE ENDOCELLULASE CELF;
D O I
10.1016/S0065-2164(10)70001-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Lignocellulose is the most abundant carbohydrate source in nature and represents an ideal renewable energy source. Thermostable enzymes that hydrolyze lignocellulose to its component sugars have significant advantages for improving the conversion rate of biomass over their mesophilic counterparts. We review here the recent literature on the development and use of thermostable enzymes for the depolymerization of lignocellulosic feedstocks for biofuel production. Furthermore, we discuss the protein structure, mechanisms of thermostability, and specific strategies that can be used to improve the thermal stability of lignocellulosic biocatalysts.
引用
收藏
页码:1 / 55
页数:55
相关论文
共 50 条
  • [41] Application of thermostable enzymes for carbohydrate modification
    Wilkinson, D
    Reuter, S
    Zimmermann, W
    ZUCKERINDUSTRIE, 1997, 122 (02): : 128 - 128
  • [42] THERMOPHILIC ORGANISMS AS SOURCES OF THERMOSTABLE ENZYMES
    KRISTJANSSON, JK
    TRENDS IN BIOTECHNOLOGY, 1989, 7 (12) : 349 - 353
  • [43] New thermostable enzymes for crop fractionation
    Duchiron, F
    Legin, E
    Ladrat, C
    Gantelet, H
    Barbier, G
    INDUSTRIAL CROPS AND PRODUCTS, 1997, 6 (3-4) : 265 - 270
  • [44] Industrial production of thermostable enzymes and their application
    Nakajima, H
    Nagata, K
    Kageyama, M
    Kondo, H
    NIPPON NOGEIKAGAKU KAISHI-JOURNAL OF THE JAPAN SOCIETY FOR BIOSCIENCE BIOTECHNOLOGY AND AGROCHEMISTRY, 1997, 71 (09): : 879 - 886
  • [45] α-Amylase: An Ideal Representative of Thermostable Enzymes
    Om Prakash
    Nivedita Jaiswal
    Applied Biochemistry and Biotechnology, 2010, 160 : 2401 - 2414
  • [46] New understandings of thermostable and peizostable enzymes
    Yano, JK
    Poulos, TL
    CURRENT OPINION IN BIOTECHNOLOGY, 2003, 14 (04) : 360 - 365
  • [47] α-Amylase: An Ideal Representative of Thermostable Enzymes
    Prakash, Om
    Jaiswal, Nivedita
    APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2010, 160 (08) : 2401 - 2414
  • [48] Sucrose Hydrolytic Enzymes: Old Enzymes for New Uses as Biocatalysts for Medical Applications
    Pang, Hao
    Du, Liqin
    Pei, Jianxin
    Wei, YuTuo
    Du, Qishi
    Huang, Ribo
    CURRENT TOPICS IN MEDICINAL CHEMISTRY, 2013, 13 (10) : 1234 - 1241
  • [49] Magnetic nanoparticle-supported enzymes as recyclable biocatalysts
    Herdt, Aimee R.
    Kim, Byeong-Su
    Taton, T. Andrew
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2006, 232 : 783 - 783
  • [50] Directed evolution of enzymes: new biocatalysts for asymmetric synthesis
    Alexeeva, M
    Carr, R
    Turner, NJ
    ORGANIC & BIOMOLECULAR CHEMISTRY, 2003, 1 (23) : 4133 - 4137