SwePub
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "L773:1359 5113 srt2:(1990-1994)"

Sökning: L773:1359 5113 > (1990-1994)

  • Resultat 1-2 av 2
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
1.
  • Andersson, Mikael, et al. (författare)
  • Characterization of the Chemical and Functional Stability of DEAE Sepharose Fast Flow
  • 1993
  • Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 28:4, s. 223-230
  • Tidskriftsartikel (refereegranskat)abstract
    • The release of amines from the ion-exchange groups in DEAE Sepharose® Fast Flow has been studied under static and column conditions. The leakage compounds have been identified and quantified by gas chromatography—mass spectrometry. It was shown that the main leakage product under acidic (pH 1) and basic conditions (pH 14) was N,N,N′,N′-tetraethylethylenediamine. Three other amines were also identified, namely N,N,N′-triethylethylenediamine, diethylaminoethanol and diethylamine. The leakage of amines from DEAE Sepharose Fast Flow treated at pH 1 or 14 for 672 h at 40°C corresponds to a reduction of only 1% of the total ion-exchange capacity.The functional stability of DEAE Sepharose Fast Flow was also studied by separation of a protein mixture during repeated cleaning-in-place treatments with 0·10 m HCl or 1·0 m NaOH. The separation behaviour was unaltered after the gel had been treated for a total contact time of 672 h with 0·10 m HCl or 1·0 m NaOH.The clearance of ethanol from a DEAE Sepharose Fast Flow column stored in a 20% ethanol aqueous solution was also studied.
  •  
2.
  • Christakopoulos, Paul, et al. (författare)
  • Exceptionally thermostable α- and β-galactosidase from Aspergillus niger separated in one step
  • 1990
  • Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 25:6, s. 210-212
  • Tidskriftsartikel (refereegranskat)abstract
    • Extracellular alpha- and-beta-galactosidases from a strain of Aspergillus niger were separated and purified in one step by cation exchange chromatography. Both enzymes had acidic pH (3.5-4.0) and high temperature (65-degrees-C) optima and an exceptionally high thermostability. Thus, -alpha-galactosidase had an activity half-time of 104 min at 60-degrees-C whereas at the same temperature the respective value for-beta-galactosidase was 835 min. At optimum conditions of activity the apparent K(m) values of alpha- and beta-galactosidase were 0.44mM and 1.1mM respectively. Both the high temperature optima and thermostability properties of the enzymes make them particularly suitable for high temperature processes.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 1-2 av 2
Typ av publikation
tidskriftsartikel (2)
Typ av innehåll
refereegranskat (2)
Författare/redaktör
Christakopoulos, Pau ... (1)
Kekos, D. (1)
Macris, B.J. (1)
Andersson, Mikael (1)
Drevin, Ingrid (1)
Johansson, Bo-Lennar ... (1)
Lärosäte
Uppsala universitet (1)
Luleå tekniska universitet (1)
Språk
Engelska (2)
Forskningsämne (UKÄ/SCB)
Naturvetenskap (1)

År

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy