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Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes beta-2,6-fructans.

Oat (Avena sativa cv Fulghum) fructan hydrolase was purified by ammonium sulfate precipitation and anion-exchange, hydrophobic interaction, and size-exclusion chromatography. The enzyme was purified to homogeneity as determined by the presence of a single band (43 kD) on a silver-stained sodium dode...

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Détails bibliographiques
Auteurs principaux: Henson, C A, Livingston, D P
Format: Artigo
Langue:Inglês
Publié: 1996
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC157760/
https://ncbi.nlm.nih.gov/pubmed/8742337
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