Effect of high substrate concentration and cell feedback on kinetic behavior of heterogeneous populations in completely mixed systems

1969 ◽  
Vol 11 (2) ◽  
pp. 207-237 ◽  
Author(s):  
M. Ramanathan ◽  
A. F. Gaudy
2004 ◽  
Vol 27 (4-6) ◽  
pp. 169-175 ◽  
Author(s):  
Ji-Heui Kim ◽  
Gi-Sub Choi ◽  
Seung-Bum Kim ◽  
Won-Ho Kim ◽  
Jin-Young Lee ◽  
...  

Catalysts ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 460
Author(s):  
Njomza Ajvazi ◽  
Stojan Stavber

N-halosuccinimides (chloro, bromo, and iodo, respectively) were introduced, tested, and applied as efficient and non-metal precatalysts for C-, N-, O-, and X-nucleophilic substitution reactions of alcohols under solvent-free reaction conditions (SFRC) or under high substrate concentration reaction conditions (HCRC) efficiently and selectively, into the corresponding products.


1971 ◽  
Vol 122 (4) ◽  
pp. 557-567 ◽  
Author(s):  
W. G. Bardsley ◽  
J. S. Ashford ◽  
C. M. Hill

1. The preparation of a series of compounds derived from diamines by replacing one amino group by a dimethylsulphonium, isothiuronium, trimethylammonium, NN′-dimethylimidazolium or N-methylpyridinium species is described. 2. The behaviour of these compounds as substrates of pig kidney diamine oxidase is reported. All but the trimethylammonium compounds proved to be substrates. 3. Many of these compounds showed potent inhibition at high substrate concentration and this was studied. 4. On the basis of these and other observations a scheme for enzyme–substrate interaction is suggested.


2017 ◽  
Vol 20 (3&4) ◽  
pp. 361-372
Author(s):  
B. Suraraksa ◽  
A. Nopharatana ◽  
P. Chaiprasert ◽  
S. Bhumiratana ◽  
M. Tanticharoen

To elucidate the effect of substrate concentration on biofilm development, glucose concentrations of 500 and 1,000 mg/L were used.  At an early stage, biofilm development at both concentrations was not significantly different (P=0.621).  After removing suspended biomass at 24 operational hours, the biofilm development at high substrate concentration was higher than at lower concentration.  At 72 operational hours, the amounts of attached biomass at low and high glucose feeding were 9.04±1.17 and 28.58±2.72 g VSS/m2, respectively.  The activities of acidogens, acetogens, and methanogens at the low glucose concentration were 0.334, 0.016 and 0.003 g COD/g VSS/h, and those at the high glucose concentration were 0.145, 0.003 and 0.001 g COD/g VSS/h, respectively.  Moreover, the ratio of methanogenic activity at low glucose concentration was higher than at high glucose concentration.  The glucose utilization at low and high feeding concentrations was 33% and 27%, respectively.  These results indicated that rapid biofilm development by using high substrate concentration would be less beneficial if unbalance of methanogenic ratio was found in biofilm.


1970 ◽  
Vol 48 (10) ◽  
pp. 1498-1504 ◽  
Author(s):  
P. V. Sundaram ◽  
A. Tweedale ◽  
K. J. Laidler

Enzymes behave differently when attached to solid supports for four main reasons: (1) their conformations when they are supported may differ from those in free solution, (2) they act upon substrates in a different environment, (3) there will be partitioning of substrate between the support and the free solution, and (4) there will be effects due to diffusion of the substrate in the support. The present paper examines effects (3) and (4) and shows how rates will vary with substrate concentration. If factors (1) and (2) do not enter, rates in the limit of high substrate concentrations will be the same for the supported enzyme as in free solution. At low substrate concentrations, rates will be less for the supported enzyme if the substrate is less soluble in the support than in free solution, and the apparent Michaelis constant, Km(app.), will be greater; conversely, for higher solubility in the support, rates will be greater and Km(app.) smaller. Effect (4) leads to lower rates and higher Km(app.) values, except in the limit of high substrate concentrations. At a sufficiently low thickness of the support, depending upon the activity of the enzyme, the kinetic behavior becomes identical with that in free solution.


2007 ◽  
Vol 349 (4-5) ◽  
pp. 709-712 ◽  
Author(s):  
Harald Gröger ◽  
Claudia Rollmann ◽  
Francoise Chamouleau ◽  
Isabelle Sebastien ◽  
Oliver May ◽  
...  

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