Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley

Earl D. Mitchell, Clifford W. Houston, Steve B. Latimer

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

β-N-Acetylaminoglucohydrolase (β-2-acetylamino-2-deoxy-D-glucoside acetylaminodeoxyglucohydrolase, EC 3.2.1.30) was extracted from malted barley and purified. The partially purified preparation was free from α-and β-glucosidase, α- and β-galactosidase, α-mannosidase and β-mannosidase. This preparation was free from α-mannosidase only after affinity chromatography with p-amino-N-acetyl-β-D-glucosaminidine coupled to Sepharose. The enzyme was active between pH 3 and 6.5 and had a pH optimum at pH 5. A MW of 92000 was obtained by sodium dodecyl sulfate-acrylamide gel electrophoresis and a sedimentation coefficient of 4.65 was obtained from sedimentation velocity experiments. β-N-Acetylaminoglucohydrolase had a Km of 2.5 × 10-4 M using the p-nitrophenyl N-acetyl β-D-glucosaminidine as the substrate.

Original languageEnglish (US)
Pages (from-to)1869-1871
Number of pages3
JournalPhytochemistry
Volume15
Issue number12
DOIs
StatePublished - 1976

Keywords

  • Gramineae
  • Hordeum vulgare
  • affinity chromatography.
  • barley
  • enzyme purification
  • β-N-acetylaminoglucohydrolase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

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