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在毕赤酵母中分泌功能性甲酸脱氢酶。

Secretion of functional formate dehydrogenase in Pichia pastoris.

作者信息

Takacs Michelle, Makhlynets Olga V, Tolbert Patricia L, Korendovych Ivan V

机构信息

Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.

出版信息

Protein Eng Des Sel. 2017 Mar 1;30(3):381-386. doi: 10.1093/protein/gzx010.

DOI:10.1093/protein/gzx010
PMID:28201611
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6075411/
Abstract

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.

摘要

生物燃料是减少二氧化碳和其他温室气体排放的重要工具。先前已证明,依赖烟酰胺腺嘌呤二核苷酸(NAD+)的甲酸脱氢酶能够将二氧化碳电化学还原为甲酸盐,而甲酸盐最终可转化为甲醇。我们证实,一种经标记以便固定化的功能性酶能够由毕赤酵母持续分泌。该蛋白质能够轻易地从生长培养基中分离出来,并且其活性在较长时间内保持恒定。这是创建一个能够以最少的资源和空间生产生物燃料的自我维持系统的重要第一步。

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Biochemistry. 2016 May 17;55(19):2760-71. doi: 10.1021/acs.biochem.6b00181. Epub 2016 May 3.
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Differential secretion pathways of proteins fused to the Escherichia coli maltose binding protein (MBP) in Pichia pastoris.融合于大肠杆菌麦芽糖结合蛋白(MBP)的蛋白质在毕赤酵母中的差异分泌途径。
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Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production.毕赤酵母中的蛋白质表达:异源蛋白生产的最新成果与展望
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