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Properties of a purified thermostable glucoamylase from Aspergillus niveus

da Silva, Tony Marcio ; Maller, Alexandre ; de Lima Damásio, André Ricardo ; Michelin, Michele ; Ward, Richard John ; Hirata, Izaura Yoshico ; Jorge, João Atilio ; Terenzi, Héctor Francisco ; de Polizeli, Maria Lourdes T. M.

Journal of industrial microbiology & biotechnology, 2009-12, Vol.36 (12), p.1439-1446 [Revista revisada por pares]

Berlin/Heidelberg: Springer-Verlag

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Properties of a purified thermostable glucoamylase from Aspergillus niveus
Autor: da Silva, Tony Marcio ; Maller, Alexandre ; de Lima Damásio, André Ricardo ; Michelin, Michele ; Ward, Richard John ; Hirata, Izaura Yoshico ; Jorge, João Atilio ; Terenzi, Héctor Francisco ; de Polizeli, Maria Lourdes T. M.
Materias: Amino Acid Sequence ; Aspergillus ; Aspergillus - enzymology ; Aspergillus - metabolism ; Biochemistry ; Bioinformatics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Chromatography ; Chromatography, Gel ; Circular Dichroism ; Enzyme Stability ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Fungi ; Genetic Engineering ; Glucan 1,4-alpha-Glucosidase - chemistry ; Glucan 1,4-alpha-Glucosidase - metabolism ; Glucose ; Hot Temperature ; Hydrogen-Ion Concentration ; Inorganic Chemistry ; Life Sciences ; Microbiology ; Molecular Weight ; Original Paper ; Peptides ; Proteins ; Sodium ; Solvents ; Studies ; Temperature ; Temperature effects
Es parte de: Journal of industrial microbiology & biotechnology, 2009-12, Vol.36 (12), p.1439-1446
Notas: ObjectType-Article-2
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Descripción: A glucoamylase from Aspergillus niveus was produced by submerged fermentation in Khanna medium, initial pH 6.5 for 72 h, at 40°C. The enzyme was purified by DEAE-Fractogel and Concanavalin A-Sepharose chromatography. The enzyme showed 11% carbohydrate content, an isoelectric point of 3.8 and a molecular mass of 77 and 76 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis or Bio-Sil-Sec-400 gel filtration, respectively. The pH optimum was 5.0–5.5, and the enzyme remained stable for at least 2 h in the pH range of 4.0–9.5. The temperature optimum was 65°C and retained 100% activity after 240 min at 60°C. The glucoamylase remained completely active in the presence of 10% methanol and acetone. After 120 min hydrolysis of starch, glucose was the unique product formed, confirming that the enzyme was a glucoamylase (1,4-alpha- d -glucan glucohydrolase). The K m was calculated as 0.32 mg ml −1 . Circular dichroism spectroscopy estimated a secondary structure content of 33% α-helix, 17% β-sheet and 50% random structure, which is similar to that observed in the crystal structures of glucoamylases from other Aspergillus species. The tryptic peptide sequence analysis showed similarity with glucoamylases from A. niger, A. kawachi, A. ficcum, A. terreus, A. awamori and A. shirousami . We conclude that the reported properties, such as solvent, pH and temperature stabilities, make A. niveus glucoamylase a potentially attractive enzyme for biotechnological applications.
Editor: Berlin/Heidelberg: Springer-Verlag
Idioma: Inglés

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Properties of a purified thermostable glucoamylase from Aspergillus niveus

da Silva, Tony Marcio ; Maller, Alexandre ; de Lima Damásio, André Ricardo ; Michelin, Michele ; Ward, Richard John ; Hirata, Izaura Yoshico ; Jorge, João Atilio ; Terenzi, Héctor Francisco ; de Polizeli, Maria Lourdes T. M.

Berlin/Heidelberg: Springer-Verlag

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