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|Type:||Artigo de periódico|
|Title:||Characterization of a glucosyltransferase from Erwinia sp D12 and the conversion of sucrose into isomaltulose by immobilized cells|
|Abstract:||Erwinia sp. D12 is able to produce an isomaltulose synthase (EC 22.214.171.124) that converts sucrose into isomaltulose. The enzyme was partially Purified using a two-step chromatographic process oil DEAE-Sephadex A-50 and DEAE-Sepharose CL-6B. The molecular mass of 63 kDa was estimated by Sephadex G-200 gel filtration, and the K(m) and V(max) values determined for the enzyme were 138 mM and 9.81 mu mol/min/mg protein with Sucrose as the substrate, respectively. Enzyme activity was optimal at pH 6.0 and 40 degrees C. The glucosyltransferase was completely inhibited by Hg(2+) and Ag(+). An experimental design and response Surface methodology were used to evaluate the influences of temperature, pH and substrate concentration oil isomaltulose production from cells immobilized in chitosan. With the aid of a two-level full factorial design (2(3)-FFD), the statistical analysis of the results showed that, in the range Studied. the factors had a significant (p<0.05) effect oil isomaltulose production. The conditions that improved isomaltulose production were: temperature around 35 degrees C, pH 6.0 and Sucrose concentration lower than 40%. (C) 2009 Elsevier B.V. All rights reserved.|
|Editor:||Elsevier Science Sa|
|Citation:||Biochemical Engineering Journal. Elsevier Science Sa, v. 48, n. 2, n. 211, n. 217, 2010.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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