Catalytically active inclusion bodies (CatIBs) induced by terminally attached self-assembling coiled-coil domains: To enhance the stability of (R)-hydroxynitrile lyase

2022 ◽  
Vol 153 ◽  
pp. 109915
Author(s):  
Xiaolin Pei ◽  
Jiapao Wang ◽  
Haoteng Zheng ◽  
Qinjie Xiao ◽  
Anming Wang ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Coiled Coil ◽  
Hydroxynitrile Lyase ◽  
Self Assembling ◽  
Active Inclusion Bodies ◽  
Catalytically Active ◽  
The Stability

Tailor-made catalytically active inclusion bodies for different applications in biocatalysis

2018 ◽  
Vol 8 (22) ◽  
pp. 5816-5826 ◽  
Author(s):  
Ramona Kloss ◽  
Tobias Karmainski ◽  
Vera D. Jäger ◽  
Doris Hahn ◽  
Alexander Grünberger ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Coiled Coil ◽  
Reaction Systems ◽  
Active Inclusion Bodies ◽  
Catalytically Active

CatIB properties can be tailored to the requirements of different reaction systems using two different coiled-coil domains as fusion tags.

Catalytically-active inclusion bodies—Carrier-free protein immobilizates for application in biotechnology and biomedicine

2017 ◽  
Vol 258 ◽  
pp. 136-147 ◽  
Author(s):  
Ulrich Krauss ◽  
Vera D. Jäger ◽  
Martin Diener ◽  
Martina Pohl ◽  
Karl-Erich Jaeger
Keyword(s):  
Inclusion Bodies ◽  
Free Protein ◽  
Active Inclusion Bodies ◽  
Carrier Free ◽  
Catalytically Active

scholarly journals Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application

2020 ◽  
Vol 104 (17) ◽  
pp. 7313-7329
Author(s):  
Vera D. Jäger ◽  
Robin Lamm ◽  
Kira Küsters ◽  
Gizem Ölçücü ◽  
Marco Oldiges ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Active Inclusion Bodies ◽  
Catalytically Active

Fusion of a Coiled-Coil Domain Facilitates the High-Level Production of Catalytically Active Enzyme Inclusion Bodies

ChemCatChem ◽  
2015 ◽  
Vol 8 (1) ◽  
pp. 142-152 ◽  
Author(s):  
Martin Diener ◽  
Benita Kopka ◽  
Martina Pohl ◽  
Karl-Erich Jaeger ◽  
Ulrich Krauss
Keyword(s):  
Inclusion Bodies ◽  
Coiled Coil ◽  
Active Enzyme ◽  
Coiled Coil Domain ◽  
Catalytically Active ◽  
High Level ◽  
Level Production

scholarly journals Tailoring the properties of (catalytically)-active inclusion bodies

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
V. D. Jäger ◽  
R. Kloss ◽  
A. Grünberger ◽  
S. Seide ◽  
D. Hahn ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Active Inclusion Bodies ◽  
Catalytically Active

scholarly journals Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Ramona Kloss ◽  
Michael H. Limberg ◽  
Ursula Mackfeld ◽  
Doris Hahn ◽  
Alexander Grünberger ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Lysine Decarboxylase ◽  
E Coli ◽  
Active Inclusion Bodies ◽  
Catalytically Active

scholarly journals Thermostable adenosine 5′-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sarah Kamel ◽  
Miriam C. Walczak ◽  
Felix Kaspar ◽  
Sarah Westarp ◽  
Peter Neubauer ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Treatment ◽  
Inclusion Bodies ◽  
Specific Activity ◽  
High Thermal Stability ◽  
Active Protein ◽  
E Coli ◽  
Thermococcus Kodakarensis ◽  
Active Inclusion Bodies ◽  
Catalytically Active

AbstractCatalytically active inclusion bodies (CatIBs) produced in Escherichia coli are an interesting but currently underexplored strategy for enzyme immobilization. They can be purified easily and used directly as stable and reusable heterogenous catalysts. However, very few examples of CatIBs that are naturally formed during heterologous expression have been reported so far. Previous studies have revealed that the adenosine 5′-monophosphate phosphorylase of Thermococcus kodakarensis (TkAMPpase) forms large soluble multimers with high thermal stability. Herein, we show that heat treatment of soluble protein from crude extract induces aggregation of active protein which phosphorolyse all natural 5′-mononucleotides. Additionally, inclusion bodies formed during the expression in E. coli were found to be similarly active with 2–6 folds higher specific activity compared to these heat-induced aggregates. Interestingly, differences in the substrate preference were observed. These results show that the recombinant thermostable TkAMPpase is one of rare examples of naturally formed CatIBs.

Accelerated production and characterization of catalytically active inclusion bodies via automated workflows

2020 ◽  
Vol 92 (9) ◽  
pp. 1201-1201
Author(s):  
K. Küsters ◽  
W. Wiechert ◽  
M. Oldiges ◽  
S. Albert
Keyword(s):  
Inclusion Bodies ◽  
Active Inclusion Bodies ◽  
Catalytically Active
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