Effect of culture conditions and signal peptide on production of human recombinant N-acetylgalactosamine-6-sulfate sulfatase in Escherichia coli BL21

A Hernández, O Velásquez, F Leonardi… - … of microbiology and …, 2013 - koreascience.kr
The production and characterization of an active recombinant N-acetylgalactosamine-6-
sulfate sulfatase (GALNS) in Escherichia coli BL21 (DE3) has been previously reported. In …

Characterization of recombinant pectate lyase refolded from inclusion bodies generated in E. coli BL21 (DE3)

S Kumar, KK Jain, A Singh, AK Panda… - Protein Expression and …, 2015 - Elsevier
Abstract Pectate lyase (EC 4.2. 2.2) gene from Bacillus subtilis RCK was cloned and
expressed in Escherichia coli to maximize its production. In addition to soluble fraction …

An overview of culture conditions for recombinant protein expression in Escherichia coli

IP Maksum, FPU Latifah, A Nabiel… - Journal of Applied …, 2023 - biotechrep.ir
Escherichia coli is one of the most commonly used organisms for producing recombinant
protein. The recognized cell genome and well-known cell factory of the bacteria make it an …

[HTML][HTML] A variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies

G Raghunathan, G Munussami, H Moon, H Paik… - Microbial Cell …, 2014 - Springer
Abstract Background Inclusion bodies (IBs) were generally considered to be inactive protein
deposits and did not hold any attractive values in biotechnological applications. Recently …

[HTML][HTML] Microwave assisted solubilization of inclusion bodies

I Datta, S Gautam, MN Gupta - Sustainable Chemical Processes, 2013 - Springer
Background Production of recombinant proteins in bacterial hosts often produces insoluble
intracellular particles called inclusion bodies. Recovery of active protein from inclusion …

[HTML][HTML] Methodological advances and strategies for high resolution structure determination of cellular protein aggregates

A Schaefer, D Naser, B Siebeneichler… - Journal of Biological …, 2022 - ASBMB
Aggregation of proteins is at the nexus of molecular processes crucial to aging, disease, and
employing proteins for biotechnology and medical applications. There has been much …

Purification of viral neuraminidase from inclusion bodies produced by recombinant Escherichia coli

S Lipničanová, D Chmelová, A Godány… - Journal of …, 2020 - Elsevier
Neuraminidase (NA) is one of the targets for the development of new antivirals against the
influenza virus. The recombinant Escherichia coli cells, namely the strains BL21 (DE3) …

[HTML][HTML] Effective refolding of a cysteine rich glycoside hydrolase family 19 recombinant chitinase from Streptomyces griseus by reverse dilution and affinity …

AO Oyeleye, SF Mohd Yusoff, IN Abd Rahim… - Plos one, 2020 - journals.plos.org
Conventional refolding methods are associated with low yields due to misfolding and high
aggregation rates or very dilute proteins. In this study, we describe the optimization of the …

Bacterial suspension cultures

P Sagmeister, M Jazini, J Klein… - … scale suspension culture …, 2014 - Wiley Online Library
Bacteria became the primary workhorses of the biotechnology industry due to fast growth on
inexpensive media, well understood genetics, and an advanced genetic engineering toolset …

Characterization of the enzymes involved in the diolsynthase pathway in Pseudomonas aeruginosa

S Shoja Chaghervand - 2019 - diposit.ub.edu
[eng] In 2015 our research group described, in P. aeruginosa, the oleate-diol synthase
system which consists of two sequentially and independently enzymatic reactions: 10S …