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'Aspergillus niger' in keywords Facet   Publication Year 1980  [X]
Facet   section ZfN Section C  [X]
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1Author    B. Schöbel, W. PollmannRequires cookie*
 Title    Isolierung und Charakterisierung einer Acetylester-Hydrolase aus Aspergillus rtiger Isolation and Characterization of an Acetylester-Hydrolase from Aspergillus niger  
  Reference    Z. Naturforsch. 35c, 696—6 (1980); eingegangen am 7. Mai 1980 
  Published    1980 
  Keywords    Acetylester-Hydrolase, Aspergillus niger, Gelfiltration, Autotitration 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0696.pdf 
 Identifier    ZNC-1980-35c-0696 
 Volume    35 
2Author    B. Schöbel, W. PollmannRequires cookie*
 Title    Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger  
 Abstract    The isolation and characterization o f a specific chlorogenic acid esterase is described. The en­ zyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means o f ultrafiltration and column-chromatography. The pH-and tempe­ rature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the en­ zyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. TTie Ä Tm-value is 0.70 mM chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­ genic acid. The isoelectric focusing reveals several isoenzymes o f chlorogenase within a pl-range o f 4 .0 -4 .5 . 
  Reference    Z. Naturforsch. 35c, 209 (1980); received November 20 1979/January 17 1980 
  Published    1980 
  Keywords    Chlorogenic Acid Esterase, Aspergillus niger, High Performance Thin Layer Chromatography 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0209.pdf 
 Identifier    ZNC-1980-35c-0209 
 Volume    35 
3Author    Abteilung Biochemie, C.H Boehringer SohnRequires cookie*
 Title    B. Schöbel und W. Pollmann  
 Abstract    In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits o f the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature o f 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger 
  Reference    Z. Naturforsch. 35c, 699—701 (1980); eingegangen am 12. Mai/20. Juni 1980 
  Published    1980 
  Keywords    Chlorogenic Acid Hydrolase, Aspergillus niger, Polyacrylamid Gelelectrophoresis, Amino Acid Analysis, Substrate Specificity 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0699.pdf 
 Identifier    ZNC-1980-35c-0699 
 Volume    35