scholarly journals Formation of nicotinic acid ribonucleoside by an enzyme preparation and growing mycelium of Aspergillus niger.

1977 ◽  
Vol 41 (4) ◽  
pp. 625-629 ◽  
Author(s):  
Masaaki KUWAHARA
Keyword(s):  
Aspergillus Niger ◽  
Nicotinic Acid ◽  
Enzyme Preparation

scholarly journals Polyprenol phosphate as an acceptor of mannose from guanosine diphosphate mannose in Aspergillus niger

1972 ◽  
Vol 126 (5) ◽  
pp. 1203-1208 ◽  
Author(s):  
R. M. Barr ◽  
F. W. Hemming
Keyword(s):  
Aspergillus Niger ◽  
Enzyme Preparation ◽  
Cetyl Alcohol ◽  
Incubation Mixture ◽  
Guanosine Diphosphate

Growth of Aspergillus niger in the presence of [2-14C]mevalonate and 32Pi led to the formation of a lipid, containing 14C (0.14% of dose) and 32P (0.009% of dose), that had chromatographic properties identical with those of exo-methylene-hexahydropolyprenol phosphate. When a particulate enzyme preparation from the thallus of A. niger was incubated with GDP-[14C]mannose, the main radioactive products were mannose 1-phosphate (57% of products) and mannose (18%). In addition radioactive mannan (8%) and a mannolipid (2%) were formed. The latter was identified as exo-methylene-hexahydropolyprenol phosphate mannose on the basis of its chromatographic properties, acid lability and on the increase in formation of the mannolipid when the phosphate of exo-methylene-hexahydropolyprenols was added to the incubation mixture. The phosphates of ficaprenols and cetyl alcohol caused no corresponding increase. These observations are interpreted as evidence that the thallus of A. niger contains a mannose transferase that uses the phosphate of exo-methylene-hexahydropolyprenols as an acceptor. This situation is discussed in the light of the analogous involvement of a prenol phosphate mannose as an intermediate in the biosynthesis of bacterial wall mannan.

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

scholarly journals Preparation and immobilization Glucoamylase and Pectinase by CLEA method

2014 ◽  
Vol 17 (2) ◽  
pp. 45-51
Author(s):  
Giang Thi Linh Tran ◽  
Oanh Ngoc Huynh
Keyword(s):  
Aspergillus Niger ◽  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Solution Culture ◽  
Crude Enzyme ◽  
Cross Linking ◽  
Solid Culture ◽  
Enzyme Solution ◽  
Crude Enzyme Solution ◽  
Semi Solid

CLEA method (cross-linking enzyme aggregates) combines enzyme preparation and immobilization from solution culture into the same step. In this study, we applied CLEA method to immobilize two enzymes, glucoamylase and pectinase, from crude enzyme solution obtained from semi-solid culture of Aspergillus niger. The results showed that: In the same immobilized conditions (glucoamylase: 7% glutaraldehyde, 5°C, 2 hours; pectinase: 10% glutaraldehyde, 5°C, 2 hours), the immobilized enzyme from crude enzyme solution, has the abilities to be reused and activation stability under the influences of pH and temperature higher than immobilized commercial enzyme respectively.

scholarly journals STUDIES ON RHAMNOGALACTURONASE IN FRUIT

HortScience ◽  
1992 ◽  
Vol 27 (6) ◽  
pp. 653d-653
Author(s):  
Jongkee Kim ◽  
Kenneth C. Gross
Keyword(s):  
Cell Wall ◽  
Aspergillus Niger ◽  
Linkage Analysis ◽  
Trifluoroacetic Acid ◽  
Enzyme Preparation ◽  
Tomato Fruit ◽  
Apple Fruit ◽  
Partial Purification ◽  
Fruit Softening ◽  
Fungal Enzyme

Rhamnogalacturonase (RGase) is a new fungal enzyme which degrades the highly branched regions of apple fruit cell wall pectin by cleaving the glycosyl linkage between rhamnosyl and galacturonosyl residues (Schols et al., 1990. Carhohydr. Res. 206:105.). This enzyme, if present in fruit, could play a significant role in fruit softening. Partial purification of RGase was accomplished from a fungal enzyme preparation (Pectinex Ultra SP-L, NOVO Ferment) produced from Aspergillus niger. The crude enzyme hydrolyzed chelator-soluble pectin from red ripe tomato fruit. Methylation linkage analysis of the product suggested that an increase in terminal-rhamnosyl residues accompanied pectin hydrolysis, indicative of RGase activity. Cross-linked alginate, hydroxyapatite, and DEAE-Sephadex chromatography were used to partially purify RGase. Polygalacturonase was efficiently removed using the alginate column. Crude pectin obtained from mature-green tomato fruit cell wall by extracting with 0.5 M imidazole buffer (pH 7) and 50 mM Na-carbonate was incubated with pure polygalacturonase and the residue hydrolyzed with 0.1 N trifluoroacetic acid. This modified pectin was used as a substrate to investigate the presence of RGase in tomato and other fruit.

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