Coenzyme production using immobilized enzymes. I. Preparation, characterization, and laboratory-scale application of an immobilized NAD+ kinase

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Abstract

NAD+ kinase (ATP: NAD+ 2-phosphotransferase, EC2.7.1.23) isolated from chicken liver was immobilized on a silica-based support possessing aldehyde functional groups. The highest catalytic activity achieved was 16 U g-1 solid. The optimal pH for the catalytic activity of the immobilized NAD+ kinase was pH 7.1-7.3. The apparent optimum temperature for the immobilized enzyme was about 5°C higher than that of the soluble enzyme. There were no significant differences in the Km app values. The immobilization improved the conformational stability of the enzyme. In preliminary experiments, a 95% conversion of NAD+ to NADP+ was achieved with use of the immobilized NAD+ kinase, which preserved its starting activity practically unchanged up to 36 days.

Original languageEnglish
Pages (from-to)997-1000
Number of pages4
JournalEnzyme and Microbial Technology
Volume14
Issue number12
DOIs
Publication statusPublished - 1992

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Coenzymes
Immobilized Enzymes
Enzymes
NAD
Catalyst activity
Enzyme Stability
Adenosinetriphosphate
Aldehydes
NADP
Catalyst supports
Application programs
Silicon Dioxide
Immobilization
Liver
Functional groups
Chickens
Phosphotransferases
Adenosine Triphosphate
Silica
Temperature

Keywords

  • continuous production
  • immobilized
  • NAD kinase
  • NADP
  • silica-based support

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

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title = "Coenzyme production using immobilized enzymes. I. Preparation, characterization, and laboratory-scale application of an immobilized NAD+ kinase",
abstract = "NAD+ kinase (ATP: NAD+ 2-phosphotransferase, EC2.7.1.23) isolated from chicken liver was immobilized on a silica-based support possessing aldehyde functional groups. The highest catalytic activity achieved was 16 U g-1 solid. The optimal pH for the catalytic activity of the immobilized NAD+ kinase was pH 7.1-7.3. The apparent optimum temperature for the immobilized enzyme was about 5°C higher than that of the soluble enzyme. There were no significant differences in the Km app values. The immobilization improved the conformational stability of the enzyme. In preliminary experiments, a 95{\%} conversion of NAD+ to NADP+ was achieved with use of the immobilized NAD+ kinase, which preserved its starting activity practically unchanged up to 36 days.",
keywords = "continuous production, immobilized, NAD kinase, NADP, silica-based support",
author = "Simon, {L. M.} and M. Kotorm{\'a}n and B. Szaj{\'a}ni",
year = "1992",
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language = "English",
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journal = "Enzyme and Microbial Technology",
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T1 - Coenzyme production using immobilized enzymes. I. Preparation, characterization, and laboratory-scale application of an immobilized NAD+ kinase

AU - Simon, L. M.

AU - Kotormán, M.

AU - Szajáni, B.

PY - 1992

Y1 - 1992

N2 - NAD+ kinase (ATP: NAD+ 2-phosphotransferase, EC2.7.1.23) isolated from chicken liver was immobilized on a silica-based support possessing aldehyde functional groups. The highest catalytic activity achieved was 16 U g-1 solid. The optimal pH for the catalytic activity of the immobilized NAD+ kinase was pH 7.1-7.3. The apparent optimum temperature for the immobilized enzyme was about 5°C higher than that of the soluble enzyme. There were no significant differences in the Km app values. The immobilization improved the conformational stability of the enzyme. In preliminary experiments, a 95% conversion of NAD+ to NADP+ was achieved with use of the immobilized NAD+ kinase, which preserved its starting activity practically unchanged up to 36 days.

AB - NAD+ kinase (ATP: NAD+ 2-phosphotransferase, EC2.7.1.23) isolated from chicken liver was immobilized on a silica-based support possessing aldehyde functional groups. The highest catalytic activity achieved was 16 U g-1 solid. The optimal pH for the catalytic activity of the immobilized NAD+ kinase was pH 7.1-7.3. The apparent optimum temperature for the immobilized enzyme was about 5°C higher than that of the soluble enzyme. There were no significant differences in the Km app values. The immobilization improved the conformational stability of the enzyme. In preliminary experiments, a 95% conversion of NAD+ to NADP+ was achieved with use of the immobilized NAD+ kinase, which preserved its starting activity practically unchanged up to 36 days.

KW - continuous production

KW - immobilized

KW - NAD kinase

KW - NADP

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