Immobilization of α-chymotrypsin was done by cross-linking the enzyme with glutaraldehyde. Studies were done in a batch reactor to find out the effects of the concentrations of α-chymotrypsin and glutaraldehyde on the rate of particle formation, the final yield of the crosslinked particles, and the residual activity of the cross-linked enzyme. Both intra- and inter-molecular cross-linking play important role at different time course of the reaction. At the begining of the cross-linking reaction, the large drop in the activity is because of the intra-molecular cross-linking and later on the large increase in the particle formation is because of the inter-molecular cross-linking.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Chibata, I. (1978), Immobilized Enzymes, Research and Development, Tokyo: Kodansha ; New York : Wiley.
Jansen, E. F., Y. Tomimatsu, and A. C. Olson (1971), Arch. Biochem. Biophys., 144, 394.
Shaked, Z., and S. Wolfe (1988), Methods Enzymol., 137, 599.
St. Clair, N. L., and M. A. Navia (1992), J. Am. Chem. Soc., 114, 7314.
Tomimatsu, Y., E. F. Jansen, W. Gaffield, and A. C. Olson (1971), J. Colloid Interface Sci., 36, 51.
Torchilin, V. P., V. S. Trubetskoy, and K. J. Martinek (1983), J. Mol. Catal., 19, 291.
Wong, S. S. (1991), Chemistry of Protein Conjugation and Cross-linking, CRC Press, Boca Raton, Florida.
Wong, S. S., and L-J. C. Wong (1992), Enzyme Microb. Technol., 14, 866.
Zaborsky, O. (1973), Immobilized Enzymes, CRC Press, Cleveland, Ohio.
About this article
Cite this article
Mohapatra, S.C., Hsu, J.T. Time dependent behaviour of the cross-linking reaction of α-chymotrypsin with glutaraldehyde. Biotechnol Tech 8, 13–16 (1994). https://doi.org/10.1007/BF00207626
- Residual Activity
- Batch Reactor