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'Esterase' in keywords Facet   section ZfN Section C  [X]
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1988 (1)
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1Author    Y. Yamazaki, M.-R KulaRequires cookie*
 Title    Entwicklung neuer Plattentests zum Nachweis mikrobieller Hydrolysen von Estern und Oxidationen von 2-Hydroxycarbonsäuren Developm ent of New Plate Tests for the D etection of Microbial Hydrolysis of Esters and Oxidations of 2-HydroxycarboxyIic Acids  
 Abstract    The application o f the thin-agar-layer coated filter culture technique (Z. Naturforsch. 42c, 1082 (1987)) has been extended to the detection of ester hydrolysis and 2-hydroxyacid oxidation by microbial colonies. The former was perform ed by spraying with brom ocresol purple and the latter with a salicylhydrazide reagent. Under the optim ized conditions, the hydrolysis activity of more than 20 [imol/h • g-wet cells and the oxidation activity o f more than 40 |j.mol/h • g-wet cells were usually detected directly on the filter-plate cultures o f bacteria, yeasts and molds. 
  Reference    Z. Naturforsch. 42c, 1187—1192 (1987); received July 30 1987 
  Published    1987 
  Keywords    Esterase, M icrobial, O xidation, Indicator, Salicylhydrazide 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1187.pdf 
 Identifier    ZNC-1987-42c-1187 
 Volume    42 
2Author    P. A. Bäumker, S. Arendt, R. WiermannRequires cookie*
 Title    Metabolism of Ferulic Acid Sucrose Esters in Anthers of Tulipa cv. Apeldoorn: II. Highly Specific Degradation of the Esters by Different Esterase Activities  
 Abstract    Protein extracts from anthers of Tulipa cv. Apeldoorn catalyze the degradation of ferulic acid sucrose esters. Different products are generated when triferuloyl sucrose (TFS) and diferuloyl sucrose (DFS) were applied as substrates. By the aid of reversed-phase HPLC, TLC and spectro-scopy the products could be identified as free ferulic acid, monoferuloyl sucrose ester [feruloyl-sucrose(mono)] and two different diesters of ferulic acid and sucrose [feruloylsucrose(di) and the endogenously occurring diferuloylsucrose (DFS)]. By means of protein fractionation (chromatofocusing, anion exchange HPLC and molecular sieving HPLC), four different enzyme activities involved in the degradation process could be separated. According to their catalytic properties, they were characterized as esterases (= EA). The partially purified esterase activity I (EA I) obtained after fractionation by chromatofocus-ing catalyzes the formation of feruloylsucrose(di) and ferulic acid when TFS is used as substrate. Incubations with EA la or EA lb isolated in smaller portions lead to the same product pattern. The esterase activity II (EA II) degrades TFS to ferulic acid and DFS. DFS as substrate is only accepted by the EA I activities, in all three cases ferulic acid and feruloyl sucrose(mono) are formed as products. The kinds of different degradation reactions clearly indicate that one enzyme (= the EA II activity) catalyzes exclusively the formation of DFS from TFS. Both enzymes, EA I and EA II, exhibit a high specificity towards ferulic acid sucrose esters. Hydroxycinnamic sucrose esters with only sinapic acid moieties do not function as substrates. When enzymatically formed sucrose esters like feruloylsucrose(di), feruloylsucrose(mono) and mono-sinapoylsucrose were used as substrates, no product formation could be observed. Applying SFS as substrate, only the ferulic acid moiety was released by EA I. Further, naturally occurring esters (glucose-and CoA-esters of p-coumaric, caffeic, ferulic and sinapic acid; chlorogenic acid; BGM) tested so far were not degraded by EA I and EA II. It is assumed that these esterase activities play a specific role in the ferulic acid metabolism in Tulipa anthers. 
  Reference    Z. Naturforsch. 43c, 647—655 (1988); received May 16 1988 
  Published    1988 
  Keywords    Tulipa cv Apeldoorn, Anthers, Ferulic Acid Sucrose Esters, Degradation, Esterases 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0647.pdf 
 Identifier    ZNC-1988-43c-0647 
 Volume    43 
3Author    G. Erhild, N. Urm, Ann, D. Ieter StrackRequires cookie*
 Title    Sinapine Esterase I. Characterization of Sinapine Esterase from Cotyledons of Raphanus sativus  
 Abstract    From cotyledons o f Raphanus sativus (red radish) an esterase activity which catalyzes the hy­ drolysis o f sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optim um o f 8.5 and the apparent K m is 1.95 x 10~5 m. The enzyme is relatively insensi­ tive to both physostigm ine (eserine) {K x = 1.73 x 10-4 m) and neostigm ine (A'i = 2 .1 3 x 10-4 m). Diisopropyl fluorophosphate (D F P) showed no inhibition and diethyl /?-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 m, respectively. Choline (10~2 m) was inhibitory but acetylcholine (1 0 -2 m) stimulated the enzyme activity. 
  Reference    Z. Naturforsch. 34c, 715—720 (1979); received June 11 1979 
  Published    1979 
  Keywords    Esterase, Sinapine, Sinapic Acid Esters, Raphanus, Brassicaceae, High-Performance Liquid Chro­ matography (HPLC) 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0715.pdf 
 Identifier    ZNC-1979-34c-0715 
 Volume    34