Thermostable glucose-tolerant glucoamylase produced by the thermophilic fungus Scytalidium thermophilum

• Published in: Folia microbiologica Vol. 46; no. 1; pp. 11 - 16
• Main Authors: Aquino, A.C.M.M, Jorge, J.A, Terenzi, H.F, Polizeli, M.L.T.M. (Universidade de Sao Paulo (Brazil). Departamento de Biologia)
• Format: Journal Article
• Language: English
• Published: Praha Academia 01.01.2001
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; AMILOPECTINA; AMILOSA; AMYLOPECTIN; AMYLOPECTINE; AMYLOSE; Ascomycota - enzymology; Ascomycota - growth & development; Bacteriology; BARIO; BARIUM; BARYUM; Biological and medical sciences; CHROMATOGRAPHIE SUR GEL; CINC; CROMATOGRAFIA SOBRE GEL; CULTURE MEDIA; ELECTROFORESIS; ELECTROPHORESE; ELECTROPHORESIS; ENZYME ACTIVITY; ENZYME INHIBITORS; Enzyme Stability; ESTABILIDAD; Fundamental and applied biological sciences. Psychology; GEL CHROMATOGRAPHY; GLICOGENO; GLICOPROTEINAS; Glucan 1,4-alpha-Glucosidase - chemistry; Glucan 1,4-alpha-Glucosidase - isolation & purification; Glucan 1,4-alpha-Glucosidase - metabolism; GLUCOAMILASA; GLUCOAMYLASE; GLUCOSA; GLUCOSE; Glucose - metabolism; GLYCOGEN; GLYCOGENE; GLYCOPROTEINE; GLYCOPROTEINS; HEAT TOLERANCE; HIDROLISIS; Human mycoses; HYDROLYSE; HYDROLYSIS; Infectious diseases; INHIBIDORES DE ENZIMAS; INHIBITEUR D'ENZYME; ISOELECTRIC POINT; Kinetics; MAGNESIO; MAGNESIUM; MALTOSA; MALTOSE; MANGANESE; MANGANESO; Medical sciences; MEDIO DE CULTIVO; Microbiology; MILIEU DE CULTURE; MOLECULAR WEIGHT; Mycoses; Mycoses of the skin; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; PESO MOLECULAR; POIDS MOLECULAIRE; POINT ISOELECTRIQUE; PUNTO ISOELECTRICO; PURIFICACION; PURIFICATION; SCYTALIDIUM; SORBITOL; STABILITE; STABILITY; Substrate Specificity; TEMPERATURA; TEMPERATURE; TEMPS; TIEMPO; TIME; TOLERANCE A LA CHALEUR; TOLERANCIA AL CALOR; ULTRAFILTRACION; ULTRAFILTRATION; ZINC; Glucan 1,4-α-glucosidase; Temperature; Thermoproteales; Archaeobacteria; Enzyme; Starch; Cellulose; Glycoprotein; Thermophily; Glucose; Maltose; Chromatography; Fungi; Ultrafiltration; Thermophilum; Glycosidases; pH; Bacteria; Hydrolases; Thermoproteaceae; Fungi Imperfecti; Scytalidium; Thallophyta
• ISSN: 0015-5632; 1874-9356
• DOI: 10.1007/BF02825876

Glucoamylase produced by Scytalidium 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 deg C and 5.5/65 deg C, respectively. The enzyme was stable for 1 h at 55 deg C and for about 8 d at 4 deg C, either at pH 7 or pH 5.5. Starch, amylopectin, glycogen, amylose and maltose were the substrates preferentially hydrolyzed. The activity was activated by 1 mmol/L Mg**2+ (27 %), Zn**2+ (21 %), Ba**2+ (8 %), Mn**2+ (5 %). Km and vlim 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.