Comparative Analysis of α-glucosidase Activity in Bombyx mori and Antheraea yamamai
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α-Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, α-glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose,sucrose, trehalose, and p-nitrophenyl α-D-glucopyranoside as substrates. In general, hemolymph α-glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut α-glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. α-Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl α-D-glucoside (MUG) indicated that the α-glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to α-glucosidase activity from A. yamamai, α-glucosidase activity from B. mori was generally less sensitive to the α-glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose,sucrose, and trehalose.
Abstract
α-Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, α-glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose,sucrose, trehalose, and p-nitrophenyl α-D-glucopyranoside as substrates. In general, hemolymph α-glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut α-glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. α-Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl α-D-glucoside (MUG) indicated that the α-glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to α-glucosidase activity from A. yamamai, α-glucosidase activity from B. mori was generally less sensitive to the α-glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose,sucrose, and trehalose.
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