PERMEABILIZATION OF BAKERS-YEAST BY CETYLTRIMETHYLAMMONIUM BROMIDE FOR INTRACELLULAR ENZYME CATALYSIS

Whole cells of Bakers' yeast (Saccharomyces cerevisiae) were permeabilized to a number of low-molecular-weight compounds by cetyltrimethylammonium bromide (CTAB). The activities of intracellular enzymes-alcohol dehydrogenase (ADH), glucose-6-phosphate dehydrogenase (G6PDH), and hexokinase-are significantly higher in the permeabilized cells and also greater than those in the cell-free extract. Maximum enzyme activities were observed when the cells were treated with CTAB (2% of wet weight of cells) at 24-degrees-C for 15 min. Permeabilization is dependent on the ratio of the detergent to the cells rather than its concentration in the medium. Properties of ADH activity of permeabilized cells were similar to those of isolated enzyme (cell-free extract). Potential use of CTAB-permeabilized cells for measuring total intracellular enzyme activity and as an alternate biocatalyst for analytical and preparative purpose has been suggested.