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

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

Research output: Contribution to journalArticle

6 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Mannosidases
mannosidases
Hordeum
Purification
barley
Sedimentation
Galactosidases
Glucosidases
galactosidases
Affinity chromatography
beta-N-acetylhexosaminidase
glucosidases
Acrylamide
acrylamides
Glucosides
sodium dodecyl sulfate
affinity chromatography
Electrophoresis
Affinity Chromatography
Sodium Dodecyl Sulfate

Keywords

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

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery

Cite this

Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley. / Mitchell, Earl D.; Houston, Clifford W.; Latimer, Steve B.

In: Phytochemistry, Vol. 15, No. 12, 1976, p. 1869-1871.

Research output: Contribution to journalArticle

Mitchell, Earl D. ; Houston, Clifford W. ; Latimer, Steve B. / Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley. In: Phytochemistry. 1976 ; Vol. 15, No. 12. pp. 1869-1871.
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N2 - 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.

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