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

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

doi:10.1016/S0031-9422(00)88833-0

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

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

Research output: Contribution to journal › Article › peer-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 K_m of 2.5 × 10^-4 M using the p-nitrophenyl N-acetyl β-D-glucosaminidine as the substrate.

Original language	English (US)
Pages (from-to)	1869-1871
Number of pages	3
Journal	Phytochemistry
Volume	15
Issue number	12
DOIs	https://doi.org/10.1016/S0031-9422(00)88833-0
State	Published - 1976
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Plant Science
Horticulture

Access to Document

10.1016/S0031-9422(00)88833-0

Cite this

@article{61f36641842d4f25b7228de903c1f0f9,

title = "Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley",

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.",

keywords = "Gramineae, Hordeum vulgare, affinity chromatography., barley, enzyme purification, β-N-acetylaminoglucohydrolase",

author = "Mitchell, {Earl D.} and Houston, {Clifford W.} and Latimer, {Steve B.}",

note = "Funding Information: *Journal Article Number 3128 of the Oklahoma Agricultural Experiment Station, Oklahoma State University, Stillwater, Oklahoma 74074. This research was supported in part by CSRS Research Grant from the U.S. Department of Agriculture to Langston University and in part by the Oklahoma State Agricultural Experiment Station.",

year = "1976",

doi = "10.1016/S0031-9422(00)88833-0",

language = "English (US)",

volume = "15",

pages = "1869--1871",

journal = "Phytochemistry",

issn = "0031-9422",

publisher = "Elsevier Limited",

number = "12",

}

TY - JOUR

T1 - Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley

AU - Mitchell, Earl D.

AU - Houston, Clifford W.

AU - Latimer, Steve B.

N1 - Funding Information: *Journal Article Number 3128 of the Oklahoma Agricultural Experiment Station, Oklahoma State University, Stillwater, Oklahoma 74074. This research was supported in part by CSRS Research Grant from the U.S. Department of Agriculture to Langston University and in part by the Oklahoma State Agricultural Experiment Station.

PY - 1976

Y1 - 1976

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.

AB - 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.

KW - Gramineae

KW - Hordeum vulgare

KW - affinity chromatography.

KW - barley

KW - enzyme purification

KW - β-N-acetylaminoglucohydrolase

UR - http://www.scopus.com/inward/record.url?scp=0344566247&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0344566247&partnerID=8YFLogxK

U2 - 10.1016/S0031-9422(00)88833-0

DO - 10.1016/S0031-9422(00)88833-0

M3 - Article

AN - SCOPUS:0344566247

SN - 0031-9422

VL - 15

SP - 1869

EP - 1871

JO - Phytochemistry

JF - Phytochemistry

IS - 12

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this