Abstract
Sucrose inversion may be catalyzed either by invertase or by hydrogen ions. However, acid hydrolysis by strong cation exchange resins is generally not suitable for molasses of high ion concentration. Most work with immobilized invertase has involved isolated partially purified enzymes. Johnson and Ciegler (1) have reported the entrapment of Aspergillus oryzae spores containing active invertase in ECTEOLA-cellulose for sucrose hydrolysis in a column reactor. Toda and Shoda (2) employed Saccharomyces pastorianus cells entrapped in agar pellets for inversion in a fluidized-bed reactor. In both cases relatively low substrate concentrations were used. We have previously reported on successful immobilization of S. cerevisiae yeast cells in cellulose and cellulose diacetate beads (3). We have now developed a method to obtain a stable active biocatalyst by the entrapment of invertase active yeast cells within calcium alginate gel beads.
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References
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TODA, E. & SHODA, M. Biotechnol. Bioeng. 27: 481, 1975.
LINKO, P., POUTANEN, K., WECKSTROM, L. & LINKO, Y-Y. Biochemie. (in press).
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© 1980 Plenum Press, New York
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Linko, YY., Weckstrom, L., Linko, P. (1980). Alginate Bead Entrapped Yeast Cells for Continuous Inversion of Sucrose and Molasses. In: Weetall, H.H., Royer, G.P. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3749-2_57
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DOI: https://doi.org/10.1007/978-1-4684-3749-2_57
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-3751-5
Online ISBN: 978-1-4684-3749-2
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