α-Glucosidase activities were extracted from flour of lyophilized, germinated barley seeds. To establish conditions resulting in maximal extraction of α-glucosidase activity from flour of germinated barley, we tested different buffer pH's, extraction times and temperatures, and additions of sulfhydryl reducing reagents, salts, and detergents to the extraction buffer. More enzyme activity was extracted as the extraction buffer pH increased from 3 to 9. The sulfhydryl reagents studied did not significantly increase extractable activity. The extractable activity rose with increased NaCl concentrations up to 2 M. Of the six detergents tested, the zwitterionic detergent CHAPS was most effective in solubilizing α-glucosidase activity, and when combined with NaCl resulted in a doubling in extractable activity as compared with phosphate buffer at pH 8.0. Extraction time and temperature were not critical for the actual solubilization of activity but temperature was quite critical in retaining solubilized α-glucosidase activity in crude extracts.
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Sun et al. (1992) studied this question.
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