Literature DB >> 22037492

Bacterial inclusion bodies: making gold from waste.

Elena García-Fruitós1, Esther Vázquez, César Díez-Gil, José Luis Corchero, Joaquin Seras-Franzoso, Imma Ratera, Jaume Veciana, Antonio Villaverde.   

Abstract

Many protein species produced in recombinant bacteria aggregate as insoluble protein clusters named inclusion bodies (IBs). IBs are discarded from further processing or are eventually used as a pure protein source for in vitro refolding. Although usually considered as waste byproducts of protein production, recent insights into the physiology of recombinant bacteria and the molecular architecture of IBs have revealed that these protein particles are unexpected functional materials. In this Opinion article, we present the relevant mechanical properties of IBs and discuss the ways in which they can be explored as biocompatible nanostructured materials, mainly, but not exclusively, in biocatalysis and tissue engineering.
Copyright © 2011 Elsevier Ltd. All rights reserved.

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Year:  2011        PMID: 22037492     DOI: 10.1016/j.tibtech.2011.09.003

Source DB:  PubMed          Journal:  Trends Biotechnol        ISSN: 0167-7799            Impact factor:   19.536


  45 in total

1.  Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.

Authors:  Ira Palmer; Paul T Wingfield
Journal:  Curr Protoc Protein Sci       Date:  2004-11

2.  Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.

Authors:  Ana Chen; Yamei Li; Xiuxia Liu; Quan Long; Yankun Yang; Zhonghu Bai
Journal:  J Ind Microbiol Biotechnol       Date:  2014-10-14       Impact factor: 3.346

3.  Dynamic transcriptional response of Escherichia coli to inclusion body formation.

Authors:  Faraz Baig; Lawrence P Fernando; Mary Alice Salazar; Rhonda R Powell; Terri F Bruce; Sarah W Harcum
Journal:  Biotechnol Bioeng       Date:  2014-01-30       Impact factor: 4.530

4.  Simple and Efficient Purification of Recombinant Proteins Using the Heparin-Binding Affinity Tag.

Authors:  Srinivas Jayanthi; Ravi Kumar Gundampati; Thallapuranam Krishnaswamy Suresh Kumar
Journal:  Curr Protoc Protein Sci       Date:  2017-11-01

Review 5.  Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead.

Authors:  A R Satvik Iyengar; Abhay H Pande
Journal:  Protein J       Date:  2016-12       Impact factor: 2.371

6.  Purification of Inclusion Bodies Produced in Bacteria and Yeast.

Authors:  Joaquin Seras-Franzoso; Olivia Cano-Garrido; Spela Peternel; Anna Arís; Elena Garcia-Fruitós
Journal:  Methods Mol Biol       Date:  2022

7.  Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.

Authors:  Ira Palmer; Paul T Wingfield
Journal:  Curr Protoc Protein Sci       Date:  2012-11

8.  Molecular cloning, expression, and in silico structural analysis of guinea pig IL-17.

Authors:  Vijaya R Dirisala; Amminikutty Jeevan; Suresh K Ramasamy; David N McMurray
Journal:  Mol Biotechnol       Date:  2013-11       Impact factor: 2.695

9.  Characterization of CpdC, a large-ring lactone-hydrolyzing enzyme from Pseudomonas sp. strain HI-70, and its use as a fusion tag facilitating overproduction of proteins in Escherichia coli.

Authors:  Yali Xu; Stephan Grosse; Hiroaki Iwaki; Yoshie Hasegawa; Peter C K Lau
Journal:  Appl Environ Microbiol       Date:  2013-09-13       Impact factor: 4.792

10.  Optimizing the Expression and Solubilization of an E. coli-Produced Leukemia Inhibitory Factor for Anti-LIF Antibody Production and Use Thereof for Contraception in Mice.

Authors:  Nahid Mehri; Abbas Jamshidizad; Zahra Ghanei; Ali-Asghar Karkhane; Mehdi Shamsara
Journal:  Mol Biotechnol       Date:  2021-07-16       Impact factor: 2.695

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