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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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Detalhes bibliográficos
Publicado no:Plant Physiol
Principais autores: Henson, C A, Livingston, D P
Formato: Artigo
Idioma:Inglês
Publicado em: Oxford University Press 1996
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC157760/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8742337/
https://ncbi.nlm.nih.govhttps://doi.org/10.1104/pp.110.2.639
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