scholarly journals Enzyme Encapsulation in Glycerol–Silicone Membranes for Bioreactions and Biosensors

2020 ◽  
Vol 2 (3) ◽  
pp. 1203-1212
Author(s):  
Piotr Mazurek ◽  
Paul M. Zelisko ◽  
Anne L. Skov ◽  
Michael A. Brook
1996 ◽  
Vol 15 (13) ◽  
pp. 1139-1141 ◽  
Author(s):  
S. P. Nunes ◽  
J. Schultz ◽  
K. -V. Peinemann

2018 ◽  
Vol 4 (1) ◽  
pp. 313-317 ◽  
Author(s):  
Gözde Dursun ◽  
Mersedeh Tohidnezhad ◽  
Bernd Markert ◽  
Marcus Stoffel

AbstractIt is widely known that tendon tissues are subjected to repeated cyclic mechanical load which influences cellular processes. The involvement of principles of mechanics in tissue engineering contributes to the investigations of the connection between mechanical and biological parameters in cellular processes and as well as to the development of new approaches for specific treatment methods. The healing process of injured tendons includes tenocyte migration which occurs from intact regions of tendon into the wound site. The aim of the present study is to investigate and enhance the migration characteristics of tenocytes under uniaxial mechanical stretching using an in-house tensile bioreactor system. Uniaxial mechanical stretching is applied to tenocyte-seeded silicone as well as collagen membranes, which possess different material properties. Tenocyte-seeded silicone membranes were investigated under three different loading conditions, including unstimulated (control), 3% and 5% strain, at frequency of 0.5 Hz. Tenocyte-seeded collagen membranes were investigated using three different frequencies, including unstimulated (control), 0.1 Hz and 0.5 Hz at strain of 4%. The main finding in this study is that uniaxially mechanical stretching at 3% strain enhances the cell migration more than 5% strain on silicone membranes.


2002 ◽  
Vol 14 (6) ◽  
pp. 461-463 ◽  
Author(s):  
S. Boateng ◽  
S.S. Lateef ◽  
C. Crot ◽  
D. Motlagh ◽  
T. Desai ◽  
...  

2021 ◽  
Author(s):  
Nolan W Kennedy ◽  
Carolyn E Mills ◽  
Charlotte H Abrahamson ◽  
Andre Archer ◽  
Michael C Jewett ◽  
...  

Bacterial microcompartments (MCPs) are protein-based organelles that house the enzymatic machinery for metabolism of niche carbon sources, allowing enteric pathogens to outcompete native microbiota during host colonization. While much progress has been made toward understanding MCP biogenesis, questions still remain regarding the mechanism by which core MCP enzymes are enveloped within the MCP protein shell. Here we explore the hypothesis that the shell protein PduB is responsible for linking the shell of the 1,2-propanediol utilization (Pdu) MCP from Salmonella enterica serovar Typhimurium LT2 to its enzymatic core. Using fluorescent reporters, we demonstrate that all members of the Pdu enzymatic core are encapsulated in Pdu MCPs. We also demonstrate that PduB is the sole protein responsible for linking the entire Pdu enzyme core to the MCP shell. Using MCP purifications, transmission electron microscopy, and fluorescence microscopy we find that shell assembly can be decoupled from the enzymatic core, as apparently empty MCPs are formed in Salmonella strains lacking PduB. Mutagenesis studies also reveal that PduB is incorporated into the Pdu MCP shell via a conserved, lysine-mediated hydrogen bonding mechanism. Finally, growth assays and systems-level pathway modeling reveal that unencapsulated pathway performance is strongly impacted by enzyme concentration, highlighting the importance of minimizing polar effects when conducting these functional assays. Together, these results provide insight into the mechanism of enzyme encapsulation within Pdu MCPs and demonstrate that the process of enzyme encapsulation and shell assembly are separate processes in this system, a finding that will aid future efforts to understand MCP biogenesis.


2018 ◽  
Vol 12 (1) ◽  
pp. 014107 ◽  
Author(s):  
Harpreet Matharoo ◽  
Mohammadhossein Dabaghi ◽  
Niels Rochow ◽  
Gerhard Fusch ◽  
Neda Saraei ◽  
...  

2019 ◽  
Vol 96 ◽  
pp. 171-177 ◽  
Author(s):  
María José Fabra ◽  
Zaida Pérez-Bassart ◽  
David Talens-Perales ◽  
Marta Martínez-Sanz ◽  
Amparo López-Rubio ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document