Extracellular α-glucosidase of an alkalophilic microorganism, Bacillus sp. ATCC 21591 |
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Authors: | C.T. Kelly F. O'Reilly W.M. Fogarty |
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Affiliation: | Department of Industrial Microbiology, University College, Belfield, Dublin 4, Ireland |
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Abstract: | Abstract Bacillus sp. ATCC 21591, an alkalophilic bacterium, produces 3 enzymes associated with degradation of starch-α-amylase, pullulanase and α-glucosidase. The latter reached a maximum after 24 h growth. Highest activities of α-glucosidase and pullulanase were obtained when the initial pH of the medium was 9.7 and although at pH 10.4 highest biomass was attained after 48 h no α-glucosidase was present. The pH optimum for activity with maltose as substrate was 7.0, which is surprisingly low for an alkalophilic organism. The enzyme was substrate specific for p -nitrophenyl- α -D-glucoside, maltose and maltotriose in that order. Forty eight times the activity was located in the cell-free supernatant, relative to that found intracellulary. Transferase activity was detected - the major end-product formed from maltose was a compound with an R f -value similar to isomaltose. |
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Keywords: | Neutral α-glucosidase of alkalophilic bacterium |
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