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Stabilization of soluble and immobilized horse liver alcohol dehydrogenase by adenosine 5′‐monophosphate
Author(s) -
Görisch Helmut,
Schneider Manfred
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260260827
Subject(s) - alcohol dehydrogenase , chemistry , sepharose , enzyme , adenosine monophosphate , biochemistry , dehydrogenase , horse , immobilized enzyme , agarose , alcohol , chromatography , biology , paleontology
Abstract Horse liver alcohol dehydrogenase, which catalyzes oxidoreductions for a broad spectrum of substrates of organic chemical interest, was immobilized on CNBr‐activated Sepharose and on decylamine‐substituted agarose. The specific activities of the immobilized enzyme preparations were compared with the free enzyme, and the apparent K m values of the preparations were determined for a selection of substrates. At pH 9 and 60°C, soluble liver alcohol dehydrogenase was rapidly inactivated, while the enzyme immobilized on CNBr‐activated Sepharose was more stable. Adenosine monophosphate (AMP), adenosine diphosphate, and adenosine diphosphoribose protected the free and immobilized alcohol dehydrogenase against heat inactivation. On storage under a variety of conditions, AMP effectively stabilized free horse liver alcohol dehydrogenase and the immobilized preparations.