TY - JOUR
T1 - Secretion of functional formate dehydrogenase in Pichia pastoris
AU - Takacs, Michelle
AU - Makhlynets, Olga V.
AU - Tolbert, Patricia L.
AU - Korendovych, Ivan V.
N1 - Funding Information:
This work was supported by the National Science Foundation [Grant number 1332349 to I.V.K.]; the National Institute of Health [grant number GM119634 to I.V.K.]; ORAU Ralph E. Powe Junior Faculty Enhancement award and a Humboldt Fellowship to I.V.K.
Publisher Copyright:
© The Author 2017. Published by Oxford University Press.
PY - 2017/5/1
Y1 - 2017/5/1
N2 - Biofuels are an important tool for the reduction of carbon dioxide and other greenhouse emissions. NAD+-dependent formate dehydrogenase has been previously shown to be capable of the electrochemical reduction of carbon dioxide into formate, which can be ultimately converted to methanol. We established that a functional enzyme, tagged for immobilization, could be continuously secreted by Pichia pastoris. The protein can be easily separated from the growth media and its activity remains constant over an extended period of time. This is an important first step in creating a self-sustaining system capable of producing biofuels with minimal resources and space required.
AB - Biofuels are an important tool for the reduction of carbon dioxide and other greenhouse emissions. NAD+-dependent formate dehydrogenase has been previously shown to be capable of the electrochemical reduction of carbon dioxide into formate, which can be ultimately converted to methanol. We established that a functional enzyme, tagged for immobilization, could be continuously secreted by Pichia pastoris. The protein can be easily separated from the growth media and its activity remains constant over an extended period of time. This is an important first step in creating a self-sustaining system capable of producing biofuels with minimal resources and space required.
KW - Formate dehydrogenase
KW - Pichia pastoris
KW - protein engineering
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U2 - 10.1093/protein/gzx010
DO - 10.1093/protein/gzx010
M3 - Article
C2 - 28201611
AN - SCOPUS:85020096977
SN - 1741-0126
VL - 30
SP - 381
EP - 386
JO - Protein Engineering, Design and Selection
JF - Protein Engineering, Design and Selection
IS - 5
ER -