Abstract
There is a growing interest in sustainable and environmentallyfriendly solutions for the industrial manufacturing of chemicals to replace non-renewable fossil fuel-based feedstocks. Biotransformations provide an alternative methodology to traditional reactions by taking advantage of the biochemical diversity of microorganisms to provide a chemo-, regio- and enantioselectivity, which are not always available via traditional synthetic approaches. Cutinases are enzymes secreted from phytopathogens and have been proven to be useful for several different biotransformations. This review will investigate the structure and function of cutinase. Further, it will detail cutinase activity towards both natural and non-natural substrates as well as methods employed to impart stability. Finally, we will describe the different role that cutinase has played in biotransformation reactions for biotechnology applications.
Original language | English (US) |
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Title of host publication | Green Polymer Chemistry: Biocatalysis and Biomaterials |
Publisher | American Chemical Society |
Pages | 141-158 |
Number of pages | 18 |
Volume | 1043 |
ISBN (Print) | 9780841225817 |
DOIs | |
State | Published - Aug 11 2010 |
Publication series
Name | ACS Symposium Series |
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Volume | 1043 |
ISSN (Print) | 00976156 |
ISSN (Electronic) | 19475918 |
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ASJC Scopus subject areas
- Chemistry(all)
- Chemical Engineering(all)
Cite this
Biotransformations using cutinase. / Baker, Peter James; Montclare, Jin.
Green Polymer Chemistry: Biocatalysis and Biomaterials. Vol. 1043 American Chemical Society, 2010. p. 141-158 (ACS Symposium Series; Vol. 1043).Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - Biotransformations using cutinase
AU - Baker, Peter James
AU - Montclare, Jin
PY - 2010/8/11
Y1 - 2010/8/11
N2 - There is a growing interest in sustainable and environmentallyfriendly solutions for the industrial manufacturing of chemicals to replace non-renewable fossil fuel-based feedstocks. Biotransformations provide an alternative methodology to traditional reactions by taking advantage of the biochemical diversity of microorganisms to provide a chemo-, regio- and enantioselectivity, which are not always available via traditional synthetic approaches. Cutinases are enzymes secreted from phytopathogens and have been proven to be useful for several different biotransformations. This review will investigate the structure and function of cutinase. Further, it will detail cutinase activity towards both natural and non-natural substrates as well as methods employed to impart stability. Finally, we will describe the different role that cutinase has played in biotransformation reactions for biotechnology applications.
AB - There is a growing interest in sustainable and environmentallyfriendly solutions for the industrial manufacturing of chemicals to replace non-renewable fossil fuel-based feedstocks. Biotransformations provide an alternative methodology to traditional reactions by taking advantage of the biochemical diversity of microorganisms to provide a chemo-, regio- and enantioselectivity, which are not always available via traditional synthetic approaches. Cutinases are enzymes secreted from phytopathogens and have been proven to be useful for several different biotransformations. This review will investigate the structure and function of cutinase. Further, it will detail cutinase activity towards both natural and non-natural substrates as well as methods employed to impart stability. Finally, we will describe the different role that cutinase has played in biotransformation reactions for biotechnology applications.
UR - http://www.scopus.com/inward/record.url?scp=84888007123&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84888007123&partnerID=8YFLogxK
U2 - 10.1021/bk-2010-1043.ch011
DO - 10.1021/bk-2010-1043.ch011
M3 - Conference contribution
AN - SCOPUS:84888007123
SN - 9780841225817
VL - 1043
T3 - ACS Symposium Series
SP - 141
EP - 158
BT - Green Polymer Chemistry: Biocatalysis and Biomaterials
PB - American Chemical Society
ER -