Y. Kawasaki et al., REMODELED ENZYME .2. ENZYMATIC FUNCTIONS OF FATTY ACID-MODIFIED CHYMOTRYPSIN AND TRYPSIN IN AQUEOUS-ORGANIC MEDIA, Bioscience, biotechnology, and biochemistry, 58(3), 1994, pp. 512-516
In our previous paper we demonstrated that chemical modification using
the water-soluble acylating reagent, [p-hydroxy]phenyldimethylsulfoni
um methylsulfate, enabled us to introduce a variety of hydrophobic mod
ifying groups into an enzyme molecule in an aqueous medium under mild
conditions. To investigate the effects of these introducing groups on
the hydrolytic activity of the modified enzyme, chymotrypsin and tryps
in were modified with acetyl, decanoyl, lauroyl, myristoyl, and palmit
oyl groups. We found an optimum carbon chain length and an optimum mod
ification ratio for the fatty acid-modified enzyme to catalyze a hydro
lytic reaction in aqueous-organic media, and the correlation between t
he hydrolytic activity and the dispersibility in the aqueous-organic m
edia. Compared with the unmodified enzyme, the chemical modification r
educed K(m), but had no significant effect on k(cat). The chemical mod
ification seems to promote the dispersibility of the enzymes in aqueou
s-organic media, and leads to increasing the affinity of the enzyme to
a substrate.