The kinetics of the autolytic phase of growth in cultures of Aspergillus niger

1986 ◽  
Vol 94 (2) ◽  
pp. 75-78 ◽  
Author(s):  
R. Lahoz ◽  
F. Reyes ◽  
G. G�mez Alarc�n ◽  
L. Cribeiro ◽  
M. A. Junquera ◽  
...  
Author(s):  
E. Favela-Torres ◽  
M. García-Rivero ◽  
J. Cordova-López ◽  
S. Roussos ◽  
G. Viniegra-González ◽  
...  

1998 ◽  
Vol 33 (2) ◽  
pp. 103-107 ◽  
Author(s):  
E. Favela-Torres ◽  
J. Cordova-López ◽  
M. García-Rivero ◽  
M. Gutiérrez-Rojas

2005 ◽  
Vol 11 (2) ◽  
pp. 139-147 ◽  
Author(s):  
N. Batlle ◽  
J. V. Carbonell ◽  
J. M. Sendra

This work describes the determination of depolymerisation kinetics of amylose, amylopectin and maltodextrin by Aspergillus niger glucoamylase using a flow-injection analysis system with fluorimetric detection and 2- p-toluidinylnaphthalene-2-sulfonate as the fluorescent probe. Experimental data corresponding to the time evolution of the concentration of detectable substrate were fitted to a single exponential decay curve in the case of amylose (linear substrate) and to a double exponential decay curve in the case of amylopectin and maltodextrin (ramified substrates). For all the substrates assayed, the depolymerisation rates at time zero correlated well with the initial substrate and enzyme concentrations through the Michaelis-Menten hyperbola. Therefore, this methodology allowed the determination of glucoamylase activity using any of these substrates. The determined value of the enzymic constant K m was lower for amylose than for amylopectin and maltodextrin, thus reflecting the higher difficulty of glucoamylase to hydrolyse the (1,6) when compared to the (1,4) linkages. In contrast, the values obtained for the rate constant k3 were very similar for all the substrates assayed.


2009 ◽  
Vol 5 (2) ◽  
Author(s):  
Armando Robledo-Olivo ◽  
Juan C Contreras-Esquivel ◽  
Raul Rodriguez Herrera ◽  
Cristobal N Aguilar

Invertase production by Aspergillus niger in submerged culture was evaluated under different concentrations of sucrose and glucose. When the initial concentration of sucrose was increased from 6.25 to 50 gL-1, a higher biomass production (6.1 gL-1) was observed. The biomass production was increased 4 times more when a glucose-sucrose combination was used as substrate (26.31 gL-1). The strain A. niger produced extracellular beta-fructofuranosidase activity at all test concentrations of the substrate and the highest enzymatic activity (3873 UL-1) was obtained when sucrose was used at 12.5 gL-1. However, with a glucose-sucrose concentration of 25 gL-1 the beta-fructofuranosidase activity was of 23706 UL-1. The maximum rate of invertase enzyme production in presence of sucrose by Aspergillus niger in submerged culture was 3.67 UL-1h-1 at 12.5 gL-1 concentration, while in the case of glucose-sucrose mixture, it was 13.95 UL-1h-1 at a concentration of 25 gL-1. It was observed that the enzyme yield (YE/X) was 1.25 times more in presence of sucrose than with glucose-sucrose combination. In addition, the results suggested that an addition of lower concentration of glucose is a viable option to increase the enzyme secretion by the fungi.


2020 ◽  
Vol 22 (2) ◽  
pp. 67-72
Author(s):  
Justyna Miłek

AbstractThe thermal stability of enzyme-based biosensors is crucial in economic feasibility. In this study, thermal deactivation profiles of catalase Aspergillus niger were obtained at different temperatures in the range of 35°C to 70°C. It has been shown that the thermal deactivation of catalase Aspergillus niger follows the first-order model. The half-life time t1/2 of catalase Aspergillus niger at pH 7.0 and the temperature of 35°C and 70°C were 197 h and 1.3 h respectively. Additionally, t1/2 of catalase Aspergillus niger at the temperature of 5°C was calculated 58 months. Thermodynamic parameters the change in enthalpy ΔH*, the change in entropy ΔS* and the change Gibbs free energy ΔG* for the deactivation of catalase at different temperatures in the range of 35°C to 70°C were estimated. Catalase Aspergillus niger is predisposed to be used in biosensors by thermodynamics parameters obtained.


2000 ◽  
Vol 63 (10) ◽  
pp. 1404-1409 ◽  
Author(s):  
HIROSHI FUJIKAWA ◽  
SATOSHI MOROZUMI ◽  
GLEN H. SMERAGE ◽  
ARTHUR A. TEIXEIRA

Characteristics of capillary and test tube procedures for thermal inactivation kinetic analysis of microbial cells were studied for mold spores. During heating, capillaries were submerged in a water bath and test tubes were held with their caps positioned above the level of the heating medium. Thermal inactivation curves of Aspergillus niger spores in capillaries at around 60°C consisted of a shoulder and a fast linear decline, whereas curves in test tubes consisted of a shoulder, a fast linear decline, and a horizontal tail. There were no significant differences in values of the rate and the delay of fast declines in curves between the procedures. Some experiments were done to clarify the cause for tailing with test tubes. There were no tails with test tubes whose inner walls were not contaminated by A. niger spores, suggesting that tails arise from A. niger spores contaminating the inner walls of test tubes. Temperature of the inner wall at the level of a heating medium was lower than that of the medium. Further, there were no tails for test tubes submerged in the heating medium. These results showed that the reason for survival of contaminants on the upper wall of test tubes was that cells were not subjected to sufficient inactivation temperature. Finally, thermal inactivation curves of A. niger spores in capillaries at various constant temperatures were studied. Curves consisted of a shoulder and a fast linear decline at 57°C and above, whereas curves at below 57°C consisted of a shoulder, a fast linear decline, and a sloping tail.


2002 ◽  
Vol 68 (8) ◽  
pp. 4162-4167 ◽  
Author(s):  
M. Shimoda ◽  
H. Kago ◽  
N. Kojima ◽  
M. Miyake ◽  
Y. Osajima ◽  
...  

ABSTRACT The death kinetics of Aspergillus niger spores under high-pressure carbonation were investigated with respect to the concentration of dissolved CO2 (dCO2) and treatment temperature. All of the inactivation followed first-order death kinetics. The D value (decimal reduction time, or the time required for a 1-log-cycle reduction in the microbial population) in the saline carbonated at 10 MPa was 0.16 min at 52°C. The log D values were linearly related to the treatment temperature and the concentration of dCO2, but a significant interaction was observed between them.


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