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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

α-Chymotrypsin was adsorbed on solid support materials and the catalytic activity of the preparations in organic solvents was studied. The activity was highly dependent on the nature of the support material and on the amount of water present in the reaction mixture. There appears to be competition for the water in the system between the enzyme, the support material and the solvent. The support materials were characterized by measuring their ability to absorb water from water-saturated diisopropyl ether. For the quotient: (amount of water on the support)/(amount of water in the solvent) in the model system the term aquaphilicity was proposed. The activity of adsorbed chymotrypsin in diisopropyl ether decreased with increasing aquaphilicity of the support material. The same trend was observed when the activity of horse liver alcohol dehydrogenase adsorbed on different supports was measured in diisopropyl ether.

Abbreviations
Ac-Phe

N-acetyl-L-phenylalanine

Ac-Phe-OEt

N-acetyl-L-phenylalanine ethyl ester

CPG

controlled-pore glass

Aq

aquaphilicity

CP/MAS

cross-polarization and magic angle spinning

Enzymes
 

α-Chymotrypsin (EC 3.4.21.1)

 

horse liver alcohol dehydrogenase (EC 1.1.1.1)

REFERENCES

  1. Top of page
  2. Abstract
  3. REFERENCES
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