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Preparation of a NAD(H)-polymer matrix showing coenzymic function of the bound pyridine nucleotide

Larsson, Per-Olof LU and Mosbach, Klaus LU (1971) In Biotechnology and Bioengineering 13(3). p.393-398
Abstract
To a Sepharose gel the pyridine nucleotide NAD(H) has been bound using
dicyclohexyl carbodiimide. In order to improve the steric availability
of the nucleotide for added soluble enzymes such as dehydrogenases, a
spacer molecule, ε-amino caproic acid, was inserted between the
carbohydrate matrix and the nucleotide. The obtained preparation
contained 56 μmoles NAD+/g dry polymer. The obtained
matrix-bound NAD(H) was accepted as coenzyme by added lactate
dehydrogenase. These preparations were still active after storage for
several weeks at 4° C and could be used repeatedly without loss of
activity. This represents the first necessary step taken in the
preparation of compact closed... (More)
To a Sepharose gel the pyridine nucleotide NAD(H) has been bound using
dicyclohexyl carbodiimide. In order to improve the steric availability
of the nucleotide for added soluble enzymes such as dehydrogenases, a
spacer molecule, ε-amino caproic acid, was inserted between the
carbohydrate matrix and the nucleotide. The obtained preparation
contained 56 μmoles NAD+/g dry polymer. The obtained
matrix-bound NAD(H) was accepted as coenzyme by added lactate
dehydrogenase. These preparations were still active after storage for
several weeks at 4° C and could be used repeatedly without loss of
activity. This represents the first necessary step taken in the
preparation of compact closed systems consisting of
“enzyme–coenzyme–coenzyme-regenerating enzyme” bound to individual
polymer beads; such systems eliminate the need for continuous coenzyme
addition. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology and Bioengineering
volume
13
issue
3
pages
6 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0015052946
ISSN
0006-3592
DOI
10.1002/bit.260130306
language
English
LU publication?
yes
id
268f0eea-84b8-494c-82c9-5b2c7a6a1194
date added to LUP
2024-06-22 21:16:16
date last changed
2025-10-14 11:27:28
@article{268f0eea-84b8-494c-82c9-5b2c7a6a1194,
  abstract     = {{To a Sepharose gel the pyridine nucleotide NAD(H) has been bound using <br>
dicyclohexyl carbodiimide. In order to improve the steric availability <br>
of the nucleotide for added soluble enzymes such as dehydrogenases, a <br>
spacer molecule, ε-amino caproic acid, was inserted between the <br>
carbohydrate matrix and the nucleotide. The obtained preparation <br>
contained 56 μmoles NAD<sup>+</sup>/g dry polymer. The obtained <br>
matrix-bound NAD(H) was accepted as coenzyme by added lactate <br>
dehydrogenase. These preparations were still active after storage for <br>
several weeks at 4° C and could be used repeatedly without loss of <br>
activity. This represents the first necessary step taken in the <br>
preparation of compact closed systems consisting of <br>
“enzyme–coenzyme–coenzyme-regenerating enzyme” bound to individual <br>
polymer beads; such systems eliminate the need for continuous coenzyme <br>
addition.}},
  author       = {{Larsson, Per-Olof and Mosbach, Klaus}},
  issn         = {{0006-3592}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{393--398}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Preparation of a NAD(H)-polymer matrix showing coenzymic function of the bound pyridine nucleotide}},
  url          = {{http://dx.doi.org/10.1002/bit.260130306}},
  doi          = {{10.1002/bit.260130306}},
  volume       = {{13}},
  year         = {{1971}},
}