Abstract
α-Chymotrypsin was immobilized in inorganic microcapsules made of calcium silicate. In order to evaluate the performance of immobilized α-chymotrypsin, the rate of hydrolysis of N-acetyl- l-tyrosine ethyl ester (ATEE) and the thermostability of α-chymotrypsin were examined. The hydrolysis of ATEE by both free and encapsulated α-chymotrypsins apparently obeyed Michaelis-Menten kinetics. The apparent Michaelis constant in the encapsulated system nearly equaled that in the free enzyme system. The extent of decrease in maximum velocity by encapsulating α-chymotrypsin was much smaller than that by encapsulating lipase, suggesting that the hydrophilicity of the substrate is a key factor in the diffusion process through the wall due to the hydrophilic surface of the microcapsules. The thermostability of α-chymotrypsin was considerably enhanced by the microencapsulation. The half-life of encapsulated α-chymotrypsin was 23 times as long as that of the free one.
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