Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde

S. Barry; T. Griffin; D. B. Johnson

doi:10.1016/0020-711X(78)90012-5

Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde

S. Barry
, T. Griffin
, D. B. Johnson

Molecular Biosciences

University of Galway

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

7 Citations (Scopus)

Abstract

1. 1. Yeast alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose. Glutaraldehyde cross-linkage was required to eliminate enzyme desorption which occurred in the presence of NAD⁺. 2. 2. The immobilized enzyme was less stable than the soluble enzyme at 20°C. 3. 3. Albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme.

Original language	English
Pages (from-to)	289-292
Number of pages	4
Journal	International Journal of Biochemistry
Volume	9
Issue number	4
DOIs	https://doi.org/10.1016/0020-711X(78)90012-5
Publication status	Published - 1978

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title = "Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde",

abstract = "1. 1. Yeast alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose. Glutaraldehyde cross-linkage was required to eliminate enzyme desorption which occurred in the presence of NAD+. 2. 2. The immobilized enzyme was less stable than the soluble enzyme at 20°C. 3. 3. Albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme.",

author = "S. Barry and T. Griffin and Johnson, \{D. B.\}",

year = "1978",

doi = "10.1016/0020-711X(78)90012-5",

language = "English",

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pages = "289--292",

journal = "International Journal of Biochemistry",

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T1 - Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde

AU - Barry, S.

AU - Griffin, T.

AU - Johnson, D. B.

PY - 1978

Y1 - 1978

N2 - 1. 1. Yeast alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose. Glutaraldehyde cross-linkage was required to eliminate enzyme desorption which occurred in the presence of NAD+. 2. 2. The immobilized enzyme was less stable than the soluble enzyme at 20°C. 3. 3. Albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme.

AB - 1. 1. Yeast alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose. Glutaraldehyde cross-linkage was required to eliminate enzyme desorption which occurred in the presence of NAD+. 2. 2. The immobilized enzyme was less stable than the soluble enzyme at 20°C. 3. 3. Albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme.

UR - https://www.scopus.com/pages/publications/0017862097

U2 - 10.1016/0020-711X(78)90012-5

DO - 10.1016/0020-711X(78)90012-5

M3 - Article

C2 - 417954

AN - SCOPUS:0017862097

SN - 0020-711X

VL - 9

SP - 289

EP - 292

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

IS - 4

ER -

Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde

Abstract

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