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Literature summary for 4.1.1.1 extracted from

  • Matsuda, T.; Nakayama, K.; Abe, T.; Mukouyama, M.
    Stabilization of pyruvate decarboxylase under a pressurized carbon dioxide/water biphasic system (2010), Biocatal. Biotransform., 28, 167-171.
No PubMed abstract available

General Stability

General Stability Organism
the enzyme in phosphate buffer pressurized with CO2 up to 9 MPa for 1 h at 35°C loses most of its activity. Although the residual activity is higher in MES buffer than in phosphate buffer, deactivation cannot be prevented. With 0.7 M glycerol, the residual activity is double that without additives, and with 1-1.2 M trehalose, the residual activity is 1.5times that without additives. The stability of the enzyme is improved dramatically by immobilization onto the ion-exchange polymer Mukouyama 2000, the biocatalytic activity is fully retained even after treatment at 11 MPa. The stability of the enzyme immobilized on Toyonite-200 is lower than that of free enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
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Saccharomyces cerevisiae acetaldehyde + CO2
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r

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Saccharomyces cerevisiae