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Optimization of accessible catalase activity in polyacrylamide gel‐immobilized Saccharomyces cerevisiae
Author(s) -
Seip John E.,
Di Cosimo Robert
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260400512
Subject(s) - catalase , saccharomyces cerevisiae , yeast , polyacrylamide , polyacrylamide gel electrophoresis , chemistry , biochemistry , enzyme , chromatography , bromide , polymer chemistry , inorganic chemistry
The permeabilization of Saccharomyces cerevisiae (baker's yeast), either before or after immobilization in polyacrylamide gel (PAG), has been examined as a means to increase the catalase activity of PAG‐immobilized yeast cells. Prior permeabilization of the cells resulted in large losses of catalase activity during immobilization, but permeabilization after immobilization produced increases in the catalase activity of yeast/PAG particles. A dependence of the accessible catalase activity on the concentration of polyacrylamide in permeabilized yeast/PAG particles, and on the method of permeabilization of the immobilized cells, was observed. Optimal levels of stable catalase activity (1000–2000 IU/g PAG particles; ca. 5%–10% of total available activity) were obtained by immobilizing yeast cells (0.5 g wet cells/mL gel) in 10% (w/v) PAG, followed by permeabilization of the entrapped cells with either cetyltrimethylammonium bromide, Triton X‐100 and one freeze‐thaw, or five freeze‐thaw cycles. © 1992 John Wiley & Sons, Inc.