Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/8819

TítuloGalacto-oligosaccharides production during lactose hydrolysis by free Aspergillus oryzae β-galactosidase and immobilized on magnetic polysiloxane-polyvinyl alcohol
Autor(es)Neri, D. F. M.
Balcão, V. M.
Costa, Rafael S.
Rocha, I.
Ferreira, Eugénio C.
Torres, D.
Rodrigues, L. R.
Carvalho Junior, L. B.
Teixeira, J. A.
Palavras-chaveGalacto-oligosaccharides
Aspergillus oryzae
β-galactosidase
Covalent immobilization
Magnetic polysiloxane-polyvinyl alcohol
Mathematical modelling
beta-galactosidase
Data2009
EditoraElsevier Ltd.
RevistaFood Chemistry
CitaçãoNeri, D. F. M., Balcão, V. M., Costa, R. S., Rocha, I. C. A. P., Ferreira, E. M. F. C., Torres, D. P. M., … Teixeira, J. A. (2009, July). Galacto-oligosaccharides production during lactose hydrolysis by free Aspergillus oryzae β-galactosidase and immobilized on magnetic polysiloxane-polyvinyl alcohol. Food Chemistry. Elsevier BV. http://doi.org/10.1016/j.foodchem.2008.11.068
Resumo(s)The synthesis of galacto-oligosaccharides (GOS) by the action of Aspergillus oryzae β-galactosidase free and immobilized on magnetic polysiloxane-polyvinyl alcohol (mPOS-PVA) was studied. A maximum GOS concentration of 26% (w/v) of total sugars was achieved at near 55% lactose conversion from 50%, w/v lactose solution at pH 4.5 and 40 °C. Trisaccharides accounted for more than 81% of the total GOS produced. GOS formation was not considerably affected by pH and temperature. The concentrations of glucose and galactose encountered near maximum GOS concentration greatly inhibited the reactions and reduced GOS yield. GOS formation was not affected by enzyme immobilization in the mPOS-PVA matrix, indicating the absence of diffusional limitations in the enzyme carrier. Furthermore, this water insoluble magnetic derivative was reutilized 10-times and retained about 84% of the initial activity. In addition, the kinetic parameters for various initial lactose concentrations were determined and compared for the free and immobilized enzyme.
TipoArtigo
URIhttps://hdl.handle.net/1822/8819
DOI10.1016/j.foodchem.2008.11.068
ISSN0308-8146
Versão da editorahttps://www.sciencedirect.com/science/article/pii/S030881460801412X
Arbitragem científicayes
AcessoAcesso aberto
Aparece nas coleções:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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