α-d-Glucosidase in the midgut of the american cockroach, Periplaneta Americana

Chihiro Katagiri

Insect Biochemistry 9(2): 205-209

1979


DOI: 10.1016/0020-1790(79)90052-0
Accession: 061564924

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Abstract
A sugar-hydrolyzing enzyme was purified from the midgut of the American cockroach by DEAE-cellulose and affinity column chromatography. Examination of its substrate specificity showed that this enzyme is an α-d-glucosidase (E. C.3.2.1.20). The purified enzyme preparation exhibited a high degree of homogeneity on an acrylamide gel. However, it appeared that the preparation was still contaminated with other glycosidases such as trehalase (E. C.3.2.1.28), β-d-glucosidase (E. C.3.2.1.21) or α-amylase (E. C.3.2.1.1). The isoelectric point of the enzyme is very low, p H 3.54, the p H optimum is 5.8 and the Km value is 5.0 m M for p-nitrophenyl-α-d-glucopyranoside p- nitrophenyl-α- d -glucopyranoside. These characteristics show that the midgut α-d-glucosidase is distinct from the serum of α-d-glucosidase.