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Simple monitoring of cell leakiness and viability in bioprocesses-A case study.生物过程中细胞渗漏和活力的简单监测——一个案例研究
Eng Life Sci. 2017 Feb 1;17(6):598-604. doi: 10.1002/elsc.201600204. eCollection 2017 Jun.
2
How to trigger periplasmic release in recombinant : A comparative analysis.如何触发重组体中的周质释放:一项比较分析。
Eng Life Sci. 2016 Oct 5;17(2):215-222. doi: 10.1002/elsc.201600168. eCollection 2017 Feb.
3
Escherichia coli "TatExpress" strains super-secrete human growth hormone into the bacterial periplasm by the Tat pathway.大肠杆菌“TatExpress”菌株通过Tat途径将人生长激素超分泌到细菌周质中。
Biotechnol Bioeng. 2017 Dec;114(12):2828-2836. doi: 10.1002/bit.26434. Epub 2017 Oct 6.
4
Quantitative Evaluation of Recombinant Protein Packaged into Outer Membrane Vesicles of Escherichia coli Cells.对包装到大肠杆菌细胞外膜囊泡中的重组蛋白进行定量评估。
Biotechnol Prog. 2018 Jan;34(1):51-57. doi: 10.1002/btpr.2536. Epub 2017 Aug 21.
5
A novel method to recover inclusion body protein from recombinant E. coli fed-batch processes based on phage ΦX174-derived lysis protein E.一种基于噬菌体ΦX174来源的裂解蛋白E从重组大肠杆菌补料分批培养过程中回收包涵体蛋白的新方法。
Appl Microbiol Biotechnol. 2017 Jul;101(14):5603-5614. doi: 10.1007/s00253-017-8281-x. Epub 2017 Apr 20.
6
Application of an E. coli signal sequence as a versatile inclusion body tag.将大肠杆菌信号序列用作通用的包涵体标签。
Microb Cell Fact. 2017 Mar 21;16(1):50. doi: 10.1186/s12934-017-0662-4.
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Cytoplasmic versus periplasmic expression of site-specifically and bioorthogonally functionalized nanobodies using expressed protein ligation.利用表达蛋白连接技术实现位点特异性和生物正交功能化纳米抗体的胞质表达与周质表达
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8
An Engineered Survival-Selection Assay for Extracellular Protein Expression Uncovers Hypersecretory Phenotypes in Escherichia coli.一种用于细胞外蛋白表达的工程化生存选择测定法揭示了大肠杆菌中的高分泌表型。
ACS Synth Biol. 2017 May 19;6(5):875-883. doi: 10.1021/acssynbio.6b00366. Epub 2017 Feb 16.
9
Enhanced extracellular production of recombinant proteins in Escherichia coli by co-expression with Bacillus cereus phospholipase C.通过与蜡样芽孢杆菌磷脂酶C共表达提高大肠杆菌中重组蛋白的胞外产量。
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来自……的重组蛋白分泌

Secretion of recombinant proteins from .

作者信息

Kleiner-Grote Gabriele R M, Risse Joe M, Friehs Karl

机构信息

Fermentation Engineering Bielefeld University Bielefeld Germany.

Center for Biotechnology Bielefeld University Bielefeld Germany.

出版信息

Eng Life Sci. 2018 Apr 14;18(8):532-550. doi: 10.1002/elsc.201700200. eCollection 2018 Aug.

DOI:10.1002/elsc.201700200
PMID:32624934
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6999260/
Abstract

The microorganism is commonly used for recombinant protein production. Despite several advantageous characteristics like fast growth and high protein yields, its inability to easily secrete recombinant proteins into the extracellular medium remains a drawback for industrial production processes. To overcome this limitation, a multitude of approaches to enhance the extracellular yield and the secretion efficiency of recombinant proteins have been developed in recent years. Here, a comprehensive overview of secretion mechanisms for recombinant proteins from is given and divided into three main sections. First, the structure of the cell envelope and the known natural secretion systems are described. Second, the use and optimization of different one- or two-step secretion systems for recombinant protein production, as well as further permeabilization methods are discussed. Finally, the often-overlooked role of cell lysis in secretion studies and its analysis are addressed. So far, effective approaches for increasing the extracellular protein concentration to more than 10 g/L and almost 100% secretion efficiency exist, however, the large range of optimization methods and their combinations suggests that the potential for secretory protein production from has not yet been fully realized.

摘要

这种微生物常用于重组蛋白生产。尽管它具有生长迅速和蛋白产量高等若干优势特性,但其难以将重组蛋白轻松分泌到细胞外培养基中的问题仍是工业生产过程中的一个缺陷。为克服这一限制,近年来已开发出多种提高重组蛋白细胞外产量和分泌效率的方法。在此,对来自[微生物名称未明确]的重组蛋白分泌机制进行全面概述,并分为三个主要部分。首先,描述[微生物名称未明确]的细胞膜结构和已知的天然分泌系统。其次,讨论用于重组蛋白生产的不同一步或两步分泌系统的使用和优化,以及进一步的通透化方法。最后,阐述细胞裂解在分泌研究中常被忽视的作用及其分析。到目前为止,存在将细胞外蛋白浓度提高到超过10 g/L且分泌效率几乎达到100%的有效方法,然而,大量的优化方法及其组合表明,来自[微生物名称未明确]的分泌蛋白生产潜力尚未得到充分实现。