title: Thermostable enzymes as biocatalysts in the biofuel industry.
abstract: 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.
authors.affiliation: Institute for Genomic Biology, University of Illinois, Urbana, Illinois, USA.
authors.forename: Carl J
authors.initials: CJ
authors.lastname: Yeoman
authors.forename: Yejun
authors.initials: Y
authors.lastname: Han
authors.forename: Dylan
authors.initials: D
authors.lastname: Dodd
authors.forename: Charles M
authors.initials: CM
authors.lastname: Schroeder
authors.forename: Roderick I
authors.initials: RI
authors.lastname: Mackie
authors.forename: Isaac K O
authors.initials: IK
authors.lastname: Cann
mesh_terms: D055162:Biocatalysis; D056804:Biofuels; D018533:Biomass; D004795:Enzyme Stability; D004950:Esterases / Q000737:chemistry / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006358:Hot Temperature; D008031:Lignin / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D056804:Biofuels; C036909:lignocellulose; D008031:Lignin; D004950:Esterases; D006026:Glycoside Hydrolases