scholarly journals Development and Characterization of an Enzyme Membrane Reactor for Fructo-Oligosaccharide Production

Membranes ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 148 ◽  
Author(s):  
Burghardt ◽  
Coletta ◽  
van der Bolt ◽  
Ebrahimi ◽  
Gerlach ◽  
...  

Fructo-oligosaccharides (FOS) are linear fructans comprising 2–5 fructose units linked to a terminal glucose residue. They are widely used as food and feed additives due to their sweetness, low calorific value, and prebiotic properties. Here we describe the synthesis of FOS catalyzed by a cell-free crude enzyme solution containing recombinant fructosyltransferase (1-FFT) produced in the yeast Kluyveromyces lactis. During the enzyme catalysis, glucose accumulates as a by-product and eventually inhibits FOS production. We therefore used an enzyme membrane reactor (EMR) to achieve the continuous removal of glucose and the simultaneous replenishment of sucrose. We observed a loss of flux during the reaction with the characteristics of complete pore blocking, probably caused by a combination of proteins (enzyme molecules) and polysaccharides (FOS). Such complex fouling mechanisms must be overcome to achieve the efficient production of FOS using EMR systems.

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
K Teichmann ◽  
D Wendner ◽  
D Bachinger ◽  
S Hessenberger ◽  
G Schatzmayr

2019 ◽  
Author(s):  
Keiei Kumon ◽  
Masahiro Higashi ◽  
Shinji Saito ◽  
Shigehiko Hayashi

Many enzyme molecules exhibit characteristic global and slow dynamics which furnish them with allostery realizing remarkable molecular functionalities more than simple chemical catalysis. However, molecular mechanism of a catalytic reaction associated with the molecular flexibility of enzymes is not well-understood. Here we report a hybrid molecular simulation study on GTPase activity of a Ras-GAP protein complex for cell signaling termination. We unveiled that extensive conformational changes of the protein complex and exclusion of internal water molecules are induced upon the transition state (TS) formation in the catalytic reaction and significantly lower the reaction activation free energy. We also revealed that tumor-related mutations perturb those conformational changes upon the TS formation, leading to reduction of the catalytic activity. The findings of the remarkably dynamic protein conformation directly linking to the catalytic reaction have broad implications for understanding of enzyme mechanism and for developments of allosteric drugs and novel catalysts.


1994 ◽  
Vol 269 (40) ◽  
pp. 24953-24958 ◽  
Author(s):  
S. Colliec-Jouault ◽  
N.W. Shworak ◽  
J. Liu ◽  
A.I. de Agostini ◽  
R.D. Rosenberg
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