Studies on glycosidases and glucanases in Thaumetopoea pityocampa larvae. Part I. Purification and some properties of an α-glucosidase

1.1. An α-glucosidase was purified from Thaumetopoea pityocampa larvae (Lepidoptera Thaumetopoeidae) by means of chromatofocusing and hydroxyapatite chromatography.2.2. It was found to be homogenous on electrofocusing.3.3. Some characteristics of the enzyme were determined: mol. wt = 190,000; pI = 3.70; optimum pH = 6.0; Km for p-nitrophenyl-α-d-glucoside = 0.5 mM, for sucrose = 2.9 mM and for maltose = 0.87 mM.4.4. The enzyme hydrolyzes also maltose and the maltooligosaccharides series up to DP = 7, turanose and kojibiose.5.5. Isomaltose, trehalose and amylose are not hydrolyzed.