Evaluation of enzymatic activity of commercial inulinase from Aspergillus niger immobilized in polyurethane foam

2013 ◽  
Vol 91 (1) ◽  
pp. 54-59 ◽  
Author(s):  
Marceli Fernandes Silva ◽  
Diane Rigo ◽  
Vinícius Mossi ◽  
Rogério Marcos Dallago ◽  
Pedro Henrick ◽  
...  
1993 ◽  
Vol 39 (3) ◽  
Author(s):  
NikolayB. Vassilev ◽  
MariaCh. Vassileva ◽  
DimitrinkaI. Spassova

2015 ◽  
Author(s):  
Helen Treichel ◽  
Simone Maria Golunski ◽  
Marceli Fernandes Silva ◽  
Edenir Tozetto Luppi ◽  
Bruna Piovesan ◽  
...  

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.


1998 ◽  
Vol 64 (11) ◽  
pp. 4446-4451 ◽  
Author(s):  
Markus Wyss ◽  
Luis Pasamontes ◽  
Roland Rémy ◽  
Josiane Kohler ◽  
Eric Kusznir ◽  
...  

ABSTRACT Enzymes that are used as animal feed supplements should be able to withstand temperatures of 60 to 90°C, which may be reached during the feed pelleting process. The thermostability properties of three histidine acid phosphatases, Aspergillus fumigatus phytase,Aspergillus niger phytase, and A. niger optimum pH 2.5 acid phosphatase, were investigated by measuring circular dichroism, fluorescence, and enzymatic activity. The phytases ofA. fumigatus and A. niger were both denatured at temperatures between 50 and 70°C. After heat denaturation at temperatures up to 90°C, A. fumigatus phytase refolded completely into a nativelike, fully active conformation, while in the case of A. niger phytase exposure to 55 to 90°C was associated with an irreversible conformational change and with losses in enzymatic activity of 70 to 80%. In contrast to these two phytases,A. niger pH 2.5 acid phosphatase displayed considerably higher thermostability; denaturation, conformational changes, and irreversible inactivation were observed only at temperatures of ≥80°C. In feed pelleting experiments performed at 75°C, the recoveries of the enzymatic activities of the three acid phosphatases were similar (63 to 73%). At 85°C, however, the recovery of enzymatic activity was considerably higher for A. fumigatusphytase (51%) than for A. niger phytase (31%) or pH 2.5 acid phosphatase (14%). These findings confirm that A. niger pH 2.5 acid phosphatase is irreversibly inactivated at temperatures above 80°C and that the capacity of A. fumigatus phytase to refold properly after heat denaturation may favorably affect its pelleting stability.


FEBS Journal ◽  
2020 ◽  
Vol 287 (15) ◽  
pp. 3315-3327 ◽  
Author(s):  
Petr Pachl ◽  
Jana Kapešová ◽  
Jiří Brynda ◽  
Lada Biedermannová ◽  
Helena Pelantová ◽  
...  

1999 ◽  
Vol 42 (3) ◽  
pp. 355-362 ◽  
Author(s):  
Cristóbal Aguilar ◽  
Augur Christopher ◽  
Gustavo Viniegra-González ◽  
Ernesto Favela

Six methods to determine the activity of tannase produced by Aspergillus niger Aa-20 on polyurethane foam by solid state fermentation, which included two titrimetric techniques, three spectrophotometric methods and one HPLC assay were tested and compared. All methods assayed enabled the measurement of extracellular tannase activity. However, only five were useful to evaluate intracellular tannase activity. Studies on the effect of pH on tannase extraction demonstrated that tannase activity was considerably under-estimated when its extraction was carried out at pH values below 5.5 and above 6.0. Results showed that the HPLC technique and the modified Bajpai and Patil methods presented several advantages in comparison to the other methods tested.


2011 ◽  
Vol 165 (5-6) ◽  
pp. 1141-1151 ◽  
Author(s):  
Erika L. Ramos ◽  
Marco A. Mata-Gómez ◽  
Luis V. Rodríguez-Durán ◽  
Ruth E. Belmares ◽  
Raúl Rodríguez-Herrera ◽  
...  

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