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.

Original languageEnglish (US)
Pages (from-to)1-55
Number of pages55
JournalAdvances in applied microbiology
Volume70
DOIs
StatePublished - 2010

Fingerprint

Biofuels
Industry
Enzymes
Renewable Energy
Biomass
Hot Temperature
Carbohydrates
Proteins
lignocellulose

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology

Cite this

Thermostable enzymes as biocatalysts in the biofuel industry. / Yeoman, Carl J.; Han, Yejun; Dodd, Dylan; Schroeder, Charles M; Mackie, Roderick Ian; Cann, Isaac.

In: Advances in applied microbiology, Vol. 70, 2010, p. 1-55.

Research output: Contribution to journalReview article

@article{46be4d5f823d4984b80741a728a8c661,
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.",
author = "Yeoman, {Carl J.} and Yejun Han and Dylan Dodd and Schroeder, {Charles M} and Mackie, {Roderick Ian} and Isaac Cann",
year = "2010",
doi = "10.1016/S0065-2164(10)70001-0",
language = "English (US)",
volume = "70",
pages = "1--55",
journal = "Advances in Applied Microbiology",
issn = "0065-2164",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Thermostable enzymes as biocatalysts in the biofuel industry.

AU - Yeoman, Carl J.

AU - Han, Yejun

AU - Dodd, Dylan

AU - Schroeder, Charles M

AU - Mackie, Roderick Ian

AU - Cann, Isaac

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=77951630910&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951630910&partnerID=8YFLogxK

U2 - 10.1016/S0065-2164(10)70001-0

DO - 10.1016/S0065-2164(10)70001-0

M3 - Review article

C2 - 20359453

AN - SCOPUS:77951630910

VL - 70

SP - 1

EP - 55

JO - Advances in Applied Microbiology

JF - Advances in Applied Microbiology

SN - 0065-2164

ER -