Kinetics of amino acid esterification catalyzed by hydrophobic derivatives of alpha-chymotrypsin.
Hexyl-alpha-chymotrypsin, a hydrophobic derivative of the enzyme, is explored for the proteinase-catalyzed ester synthesis reaction with N-acetyl-L-tyrosine and ethanol. To guarantee the preservation of the enzyme activity and to allow for the extraction of the product in the organic phase, a biphasic system was used. The Vm increased for the modified enzyme. This phenomenon was linked to the modification of the protein as demonstrated by its chemical denaturation with sodium dodecyl sulfate.
D000447:Aldehydes; D000596:Amino Acids / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000378:metabolism*; D007700:Kinetics; D011489:Protein Denaturation; D012967:Sodium Dodecyl Sulfate; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D000447:Aldehydes; D000596:Amino Acids; D012967:Sodium Dodecyl Sulfate; D014443:Tyrosine; C007651:ethyl N-alpha-acetyl-tyrosinate; C010463:n-hexanal; D002918:Chymotrypsin