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Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626 by Quang D Nguyen; Judit M Rezessy-Szabó; Marc Claeyssens; Ingeborg Stals; Ágoston Hoschke is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626 about?
Amylolytic enzymes (␣-amylase and glucoamylase) from Thermomyces lanuginosus ATCC 34626 were purified to electrophoretic homogeneity. The molecular mass of purified ␣-amylase and glucoamylase were 61 and 75 kDa, respectively. Their pI values were calculated to be 3.5-3.6 and 4.1-4.3. The amylolytic enzymes from T. lanuginosus exhibit pH optima in the range 4.6-6.6 in the case of ␣-amylase and 4.4-5.6 in the case of glucoamylase. Both purified enzymes have temperature optima at 70 • C. Zn 2+ ions strongly inhibit both enzyme activities. Mn 2+ and Fe 2+ ions are activators in the case of glucoamylase; Ca 2+ and Ba 2+ are activators in the case of ␣-amylase. With half-life times longer than 1 day at 60 • C both enzymes prove to be thermostable in the pH range 4.5-8.5. The amylolytic enzymes from T. lanuginosus loose activities rapidly when incubated at temperature higher than 80 • C or at pH lower than 4.0. Both enzymes are found to be glycosylated; 8.5% carbohydrate in the case of ␣-amylase and 3.3% in the case of glucoamylase. The K m and V max of ␣-amylase on soluble starch were 0.68 mg/ml and 45.19 U/mg, respectively. The K m values of glucoamylase on maltose, maltotriose, maltote
Who reads Purification and characterisation of amylolytic enzymes from thermophilic fungus Thermomyces lanuginosus strain ATCC 34626?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Quang D Nguyen; Judit M Rezessy-Szabó; Marc Claeyssens; Ingeborg Stals; Ágoston Hoschke
- Publisher
- Elsevier Science; Elsevier ; Elsevier BV (ISSN 0141-0229)
- Published
- 2002
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)