Characterization of an Exoinulinase Produced by Aspergillus terreus CCT 4083 Grown on Sugar Cane Bagasse

Exoinulinase (β-d-fructan fructohydrolase, EC 3.2.1.80) secreted by Aspergillus terreus CCT4083 was obtained using sugar cane bagasse, an agroindustrial residue, as a carbon source. It was further purified from the supernatant culture in a rapid procedure. The enzyme presented 57 kDa on SDS-PAGE and...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2010-07, Vol.58 (14), p.8386-8391
Main Authors: Coitinho, Juliana B, Guimarães, Valéria M, de Almeida, Maíra N, Falkoski, Daniel L, de Queiróz, José H, de Rezende, Sebastião T
Format: Article
Language:English
Subjects:
Aspergillus - chemistry
Aspergillus - enzymology
Aspergillus - genetics
Biological and medical sciences
Culture Media - metabolism
Enzyme Stability
Food Chemistry/Biochemistry
Food industries
Food microbiology
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - isolation & purification
Fungal Proteins - metabolism
Gene Expression
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - genetics
Glycoside Hydrolases - isolation & purification
Glycoside Hydrolases - metabolism
Industrial Waste - analysis
Inulin - metabolism
Kinetics
Refuse Disposal
Saccharum - chemistry
Saccharum - microbiology
Substrate Specificity
Sugar industries
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Summary:Exoinulinase (β-d-fructan fructohydrolase, EC 3.2.1.80) secreted by Aspergillus terreus CCT4083 was obtained using sugar cane bagasse, an agroindustrial residue, as a carbon source. It was further purified from the supernatant culture in a rapid procedure. The enzyme presented 57 kDa on SDS-PAGE and 56 kDa on gel filtration chromatography. Inulin was hydrolyzed by the purified enzyme, yielding d-fructose as the main product. This enzyme showed maximum activity at pH 4.0 and 60 °C and maintained more than 90 and 75% of its original activity at 40 and 50 °C, respectively, after 3.5 h of preincubation. The K M values for inulin, sucrose, and raffinose were 11, 4.20, and 27.89 mM, respectively, and d-fructose was a competitive inhibitor (K i = 47.55 mM). The activation energies for sucrose, raffinose, and inulin were 10.4, 5.61, and 4.44 kcal/mol, respectively. The characteristics of A. terreus exoinulinase were compared to those of inulinases isolated from other organisms. The exoinulinase traits presented especially good thermostability and the ability to produce pure d-fructose, suggesting its application to the production of high-fructose syrup.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf1011159