Thermostable glucose-tolerant glucoamylase produced by the thermophilic fungusScytalidium thermophilum

Glucoamylase produced byScytalidium thermophilum was purified 80-fold by DEAE-cellulose, ultrafiltration and CM-cellulose chromatography. The enzyme is a glycoprotein containing 9.8% saccharide, pI of 8.3 and molar mass of 75 kDa (SDS-PAGE) or 60 kDa (Sepharose 6B). Optima of pH and temperature with...

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Bibliographic Details
Published in:Folia microbiologica 2001-02, Vol.46 (1), p.11-16
Main Authors: Aquino, A. C. M. M., Jorge, J. A., Terenzi, H. F., Polizeli, M. L. T. M.
Format: Article
Language:English
Subjects:
Amylopectin
Amylose
Carbohydrates
Cellulose
Enzymes
Fungi
Gel electrophoresis
Glucoamylase
Glucose
Glycogen
Glycogens
Glycoproteins
Magnesium
Maltose
Microbiology
pH effects
Proteins
Sodium lauryl sulfate
Starch
Substrates
Ultrafiltration
Zinc
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Description
Summary:Glucoamylase produced byScytalidium thermophilum was purified 80-fold by DEAE-cellulose, ultrafiltration and CM-cellulose chromatography. The enzyme is a glycoprotein containing 9.8% saccharide, pI of 8.3 and molar mass of 75 kDa (SDS-PAGE) or 60 kDa (Sepharose 6B). Optima of pH and temperature with starch or maltose as substrates were 5.5/70 °C and 5.5/65 °C, respectively. The enzyme was stable for 1 h at 55 °C and for about 8 d at 4 °C, either at pH 7.0 or pH 5.5. Starch, amylopectin, glycogen, amylose and maltose were the substrates preferentially hydrolyzed. The activity was activated by 1 mmol/L Mg2+ (27%), Zn2+ (21%), Ba2+ (8%) and Mn2+ (5%).Km and {ie11-1} values for starch and maltose were 0.21 g/L, 62 U/mg protein and 3.9 g/L, 9.0 U/mg protein, respectively. Glucoamylase activity was only slightly inhibited by glucose up to a 1 mol/L concentration.
ISSN:0015-5632
1874-9356
DOI:10.1007/BF02825876