Abstract
Using porous cellulose beads as a suitable matrix, Chen et al. (1) and Chun et al. (2) immobilized some enzymes by covalent or ionic binding, respectively; and Linko et al. (3) entrapped S. cerevisiae yeast cells within the beads. The retention of activity and the kinetic properties of β-galactosidase and E. coli mutant cells immobilized respectively on a) cellulose beads which were treated with p-benzoquinone and b) tannin by covalent binding and adsorption coupling were investigated in this work.
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References
CHEN, L. F. & TSAO, G. T. Biotechnol. Bioeng. 18: 1507 (1976).
CHUN, M., DICKOPP, G. & SERNETZ, M. J. Solid-Phase Biochem. 5: 211 (1980).
LINKO, Y-Y, POUTANEN, K., WECKSTROM, L. & LINKO, P. Enzyme Microb. Technol. 1: 26 (1979).
WATANABE, T., FUJIMURA, M., MORI, T., TOSA, T. & CHIBATA, I, J. Appl. Biochem. 1: 28 (1979).
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© 1982 Plenum Press, New York
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Hong, Y., Kwon, S., Chun, M., Sernetz, M. (1982). Immobilization of β-Galactosidase from E. Coli CSH36 and its Microbial Cells Using Cellulose Beads. In: Chibata, I., Fukui, S., Wingard, L.B. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9290-7_45
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DOI: https://doi.org/10.1007/978-1-4615-9290-7_45
Publisher Name: Springer, Boston, MA
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