Results 231 to 240 of about 55,805 (279)

Safety evaluation of the food enzyme cellulase from the genetically modified <i>Aspergillus niger</i> strain NZYM-EN. [PDF]

open access: yesEFSA J
EFSA Panel on Food Enzymes (FEZ)   +17 more
europepmc   +1 more source

Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans

Current Genetics, 1991
Aspergillus niger pectin lyases are encoded by a multigene family. The complete nucleotide sequence of the pectin lyase PLA-encoding gene pelA has been determined. Comparison of the deduced amino acid sequence with the deduced amino acid sequence of the other characterized pectin lyase, PLD, shows that the proteins share 69% amino acid identity.
Kusters-van Someren, M.A.   +3 more
openaire   +3 more sources

Degradation of Salicylate by Aspergillus niger

Nature, 1967
SALICYLATE continues to be a leading cause of accidental poisoning in the United States; in 1964 there were more than 16,000 cases of accidental aspirin ingestion among all age groups, accounting for 25.8 per cent of all accidental poisonings reported1.
L R, Krupka   +2 more
openaire   +2 more sources

An electrophoretic karyotype of Aspergillus niger

Molecular and General Genetics MGG, 1990
An electrophoretic karyotype of Aspergillus niger was obtained using contour-clamped homogeneous electric field (CHEF) gel electrophoresis. Chromosome-sized DNA was separated into four bands. Seven of the eight linkage groups could be correlated with specific chromosomal bands.
Debets, A.J.M.   +4 more
openaire   +2 more sources

THE HEXOSEMONOPHOSPHATE PATHWAY IN ASPERGILLUS NIGER

Canadian Journal of Microbiology, 1958
Enzymes of the hexosemonophosphate pathway were demonstrated in extracts obtained from Aspergillus niger grown in two types of media: a fermentation medium (molasses) and a rich growth medium (MYG). Preparations from cells grown in either medium contained a TPN-specific glucose-6-phosphate (G-6-P) dehydrogenase and a TPN-linked 6-phosphogluconate (6-P ...
M W, McDONOUGH, S M, MARTIN
openaire   +2 more sources

Properties of Aspergillus niger Catalase

The Journal of Biochemistry, 1982
Catalase from Aspergillus niger was purified to homogeneity as judged from the results of ultracentrifugation and polyacrylamide gel electrophoresis. The enzyme had a molecular weight of 385,000 as estimated from sedimentation measurements. Carbohydrate analyses showed that the catalase was a glycoprotein containing about 8.3% neutral sugar and 1.9 ...
K, Kikuchi-Torii   +3 more
openaire   +2 more sources

Galactosidases from Aspergillus niger

Archives of Biochemistry and Biophysics, 1970
Abstract α- And β- d -galactopyranosidases were purified from a commercial crude enzyme preparation (Rhozyme HP-150). Although both enzymes were still not homogeneous, they were free of other possibly interfering glycosidases. Properties of the purified enzymes were studied.
Y C, Lee, V, Wacek
openaire   +2 more sources

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