Multiple forms of glycosidases in an enzyme preparation from Aspergillus niger: Partial characterization of a β-apiosidase

1997 ◽  
Vol 21 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Ziya Günata ◽  
Isabelle Dugelay ◽  
M.J. Vallier ◽  
J.C. Sapis ◽  
C. Bayonove
Keyword(s):  
Aspergillus Niger ◽  
Enzyme Preparation ◽  
Partial Characterization ◽  
Multiple Forms

The assay and partial characterization of 3β-hydroxysteroid sulfotransferase of the hamster epididymis

1985 ◽  
Vol 63 (1) ◽  
pp. 71-76 ◽  
Author(s):  
M. Bouthillier ◽  
G. Bleau ◽  
A. Chapdelaine ◽  
K. D. Roberts
Keyword(s):  
Organic Phase ◽  
Enzyme Preparation ◽  
Enzymatic Reaction ◽  
Partial Characterization ◽  
Optimal Conditions ◽  
Steroid Nucleus ◽  
Optimum Ph ◽  
High Concentrations

Using a partially purified enzyme preparation obtained from hamster epididymis, a simple assay has been developed to measure the sulfurylation of dehydroisoandrosterone (DHA) and desmosterol in the presence of 3′-phosphoadenosine 5′-phospho[35S]sulfate ([35S]PAPS). After stopping the enzymatic reaction with methanol and KCl, the 35S-labelled steroid sulfates are readily extracted into an organic phase. Optimal conditions for the sulfurylation of the two steroids were compared; optimum pH is 8.7 for DHA and 9.8 for desmosterol. Sulfoconjugation of desmosterol increases with magnesium concentrations up to 6 mM, while 40 mM concentrations of the divalent ion are required for the optimal sulfurylation of DHA. Maximum sulfurylation of these steroids requires the presence of 15 mM cysteine. Michaelis–Menten kinetics are observed with DHA which has an apparent Km of 32 μM, while desmosterol inhibits sulfotransferase activity at high concentrations. Saturation of the enzyme with PAPS results in an allosteric behaviour. Only the 3β-hydroxyl function of the steroid nucleus appears to be an appropriate sulfate acceptor for the epididymal hydroxysteroid sulfotransferase.

Flavourzyme, an Enzyme Preparation with Industrial Relevance: Automated Nine-Step Purification and Partial Characterization of Eight Enzymes

2015 ◽  
Vol 63 (23) ◽  
pp. 5682-5693 ◽  
Author(s):  
Michael Merz ◽  
Thomas Eisele ◽  
Pieter Berends ◽  
Daniel Appel ◽  
Swen Rabe ◽  
...  
Keyword(s):  
Enzyme Preparation ◽  
Partial Characterization ◽  
Industrial Relevance

PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ENDO-POLYGALACTURONASE FROM ASPERGILLUS NIGER

2002 ◽  
Vol 26 (3) ◽  
pp. 253-265 ◽  
Author(s):  
CHUN-TENG GUO ◽  
WEI-MING XUE ◽  
TIAN-BAO CHEN ◽  
DENG WEN-HAN ◽  
PING-FAN RAO
Keyword(s):  
Aspergillus Niger ◽  
Partial Characterization

Purification and Partial Characterization of Cellulase Produced by Aspergillus niger Cultured on Vitellaria paradoxa shells

2017 ◽  
Vol 6 (2) ◽  
Author(s):  
Abdulhakeem Olarewaju Sulyman ◽  
Yusuf A Iyanda ◽  
Afolabi Olaniyi Opasola ◽  
OtunOla Adedayo ◽  
Raliat Abimbola Aladodo
Keyword(s):  
Aspergillus Niger ◽  
Specific Activity ◽  
Gel Filtration ◽  
Inoculum Size ◽  
Partial Characterization ◽  
Effect Of Temperature ◽  
Vitellaria Paradoxa ◽  
Endoglucanase Activity ◽  
Ammonium Sulphate Precipitation

This research investigated the purification and partial characterization of cellulase produced by Aspergillus niger cultured on Vitellaria paradoxa shells. Cellulase (endoglucanase) from A. niger was produced under optimum fermentation conditions at 35 °C, pH 4.7, V. paradoxa, 4 g/L, inoculum size of 10 mm and the fermentation media incubated for 120 hours. The crude endoglucanase obtained were partially purified by subjecting to ammonium sulphate precipitation, dialysis and gel filtration chromatography for further purification. The effect of temperature and pH on the activity of purified endoglucanase was determined. Cellulase was purified to 734.33 folds by Sephadex G-100 column chromatography with a specific activity and yield of 4.406 U/mg and 63.03% respectively. Fractions 4 and 7 contained the highest endoglucanase activity out of 18 fractions collected and the two fractions were pooled for further analysis. The activity of purified endoglucanase was optimum at a temperature of 40 °C and pH 5. Therefore, the purified endoglucanase produced may be explored in detergent industry.

Production and partial characterization of glucose oxidase and catalase from xerophytic strain of Aspergillus niger

2014 ◽  
Vol 8 (29) ◽  
pp. 2788-2800
Author(s):  
Vernica Garay Flores Roco ◽  
Patricia Segura Ceniceros Elda ◽  
de Len Gmez Rosalba ◽  
Balvantn Garca Cecilia ◽  
Luis Martnez Hernndez Jos ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Glucose Oxidase ◽  
Partial Characterization
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