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Beta Fructofuranosidase

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Maria Fernandezlobato – 1st expert on this subject based on the ideXlab platform

  • biochemical characterization of a Beta Fructofuranosidase from rhodotorula dairenensis with transfructosylating activity
    Fems Yeast Research, 2009
    Co-Authors: Patricia Gutierrezalonso, Francisco J Plou, Lucia Fernandezarrojo, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Rhodotorula dairenensis was characterized biochemically. The enzyme molecular mass was estimated to be 680 kDa by analytical gel filtration and 172 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of which the N-linked carbohydrate accounts for 16% of the total mass. It displays optimum activity at pH 5 and 55-60 degrees C. The enzyme shows broad substrate specificity, hydrolyzing sucrose, 1-kestose, nystose, leucrose, raffinose and inulin. Although the main reaction catalyzed by this enzyme is sucrose hydrolysis, it also exhibits transfructosylating activity that, unlike other microbial BetaFructofuranosidases, produces a varied type of prebiotic fructooligosaccharides containing Beta-(2–>1)- and Beta-(2–>6)-linked fructose oligomers. The maximum concentration of fructooligosaccharides was reached at 75% sucrose conversion and it was 87.9 g L(-1). The 17.0% (w/w) referred to the total amount of sugars in the reaction mixture. At this point, the amounts of 6-kestose, neokestose, 1-kestose and tetrasaccharides were 68.9, 10.6, 2.6 and 12.7 g L(-1), respectively.

  • molecular and biochemical characterization of a Beta Fructofuranosidase from xanthophyllomyces dendrorhous
    Applied and Environmental Microbiology, 2009
    Co-Authors: Dolores Linde, Isabel Macias, Lucia Fernandezarrojo, Francisco J Plou, Antonio J Jimenez, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Xanthophyllomyces dendrorhous was characterized biochemically, molecularly, and phylogenetically. This enzyme is a glycoprotein with an estimated molecular mass of 160 kDa, of which the N-linked carbohydrate accounts for 60% of the total mass. It displays optimum activity at pH 5.0 to 6.5, and its thermophilicity (with maximum activity at 65 to 70 degrees C) and thermostability (with a T(50) in the range 66 to 71 degrees C) is higher than that exhibited by most yeast invertases. The enzyme was able to hydrolyze fructosyl-Beta-(2–>1)-linked carbohydrates such as sucrose, 1-kestose, or nystose, although its catalytic efficiency, defined by the k(cat)/K(m) ratio, indicates that it hydrolyzes sucrose approximately 4.2 times more efficiently than 1-kestose. Unlike other microbial BetaFructofuranosidases, the enzyme from X. dendrorhous produces neokestose as the main transglycosylation product, a potentially novel bifidogenic trisaccharide. Using a 41% (wt/vol) sucrose solution, the maximum fructooligosaccharide concentration reached was 65.9 g liter(-1). In addition, we isolated and sequenced the X. dendrorhous BetaFructofuranosidase gene (Xd-INV), showing that it encodes a putative mature polypeptide of 595 amino acids and that it shares significant identity with other fungal, yeast, and plant BetaFructofuranosidases, all members of family 32 of the glycosyl-hydrolases. We demonstrate that the Xd-INV could functionally complement the suc2 mutation of Saccharomyces cerevisiae and, finally, a structural model of the new enzyme based on the homologous invertase from Arabidopsis thaliana has also been obtained.

Francisco J Plou – 2nd expert on this subject based on the ideXlab platform

  • fructosylation of hydroxytyrosol by the Beta Fructofuranosidase from xanthophyllomyces dendrorhous insights into the molecular basis of the enzyme specificity
    Chemcatchem, 2018
    Co-Authors: M Ramirezescudero, A Poveda, Antonio Ballesteros, Francisco J Plou

    Abstract:

    This work was supported by grants from the Spanish Ministry of
    Economy and Competitiveness (BIO2013-48779-C4-1/3/4 and
    BIO2016-76601-C3-1-R/2-R/3-R), by an institutional grant from
    the Fundacion Ramon Areces to the Centro de Biologia Molecular
    Severo Ochoa (CBMSO), and by the European Union’s Horizon
    2020 research and innovation program [Blue Growth: Unlocking
    the potential of Seas and Oceans] under grant agreement No
    634486 (INMARE). We thank the support of COST-Action
    CM1303 on Systems Biocatalysts. M.G-P thank the Spanish
    Ministry of Education for FPU Grant.

  • biochemical characterization of a Beta Fructofuranosidase from rhodotorula dairenensis with transfructosylating activity
    Fems Yeast Research, 2009
    Co-Authors: Patricia Gutierrezalonso, Francisco J Plou, Lucia Fernandezarrojo, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Rhodotorula dairenensis was characterized biochemically. The enzyme molecular mass was estimated to be 680 kDa by analytical gel filtration and 172 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of which the N-linked carbohydrate accounts for 16% of the total mass. It displays optimum activity at pH 5 and 55-60 degrees C. The enzyme shows broad substrate specificity, hydrolyzing sucrose, 1-kestose, nystose, leucrose, raffinose and inulin. Although the main reaction catalyzed by this enzyme is sucrose hydrolysis, it also exhibits transfructosylating activity that, unlike other microbial BetaFructofuranosidases, produces a varied type of prebiotic fructooligosaccharides containing Beta-(2–>1)- and Beta-(2–>6)-linked fructose oligomers. The maximum concentration of fructooligosaccharides was reached at 75% sucrose conversion and it was 87.9 g L(-1). The 17.0% (w/w) referred to the total amount of sugars in the reaction mixture. At this point, the amounts of 6-kestose, neokestose, 1-kestose and tetrasaccharides were 68.9, 10.6, 2.6 and 12.7 g L(-1), respectively.

  • molecular and biochemical characterization of a Beta Fructofuranosidase from xanthophyllomyces dendrorhous
    Applied and Environmental Microbiology, 2009
    Co-Authors: Dolores Linde, Isabel Macias, Lucia Fernandezarrojo, Francisco J Plou, Antonio J Jimenez, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Xanthophyllomyces dendrorhous was characterized biochemically, molecularly, and phylogenetically. This enzyme is a glycoprotein with an estimated molecular mass of 160 kDa, of which the N-linked carbohydrate accounts for 60% of the total mass. It displays optimum activity at pH 5.0 to 6.5, and its thermophilicity (with maximum activity at 65 to 70 degrees C) and thermostability (with a T(50) in the range 66 to 71 degrees C) is higher than that exhibited by most yeast invertases. The enzyme was able to hydrolyze fructosyl-Beta-(2–>1)-linked carbohydrates such as sucrose, 1-kestose, or nystose, although its catalytic efficiency, defined by the k(cat)/K(m) ratio, indicates that it hydrolyzes sucrose approximately 4.2 times more efficiently than 1-kestose. Unlike other microbial BetaFructofuranosidases, the enzyme from X. dendrorhous produces neokestose as the main transglycosylation product, a potentially novel bifidogenic trisaccharide. Using a 41% (wt/vol) sucrose solution, the maximum fructooligosaccharide concentration reached was 65.9 g liter(-1). In addition, we isolated and sequenced the X. dendrorhous BetaFructofuranosidase gene (Xd-INV), showing that it encodes a putative mature polypeptide of 595 amino acids and that it shares significant identity with other fungal, yeast, and plant BetaFructofuranosidases, all members of family 32 of the glycosyl-hydrolases. We demonstrate that the Xd-INV could functionally complement the suc2 mutation of Saccharomyces cerevisiae and, finally, a structural model of the new enzyme based on the homologous invertase from Arabidopsis thaliana has also been obtained.

Lucia Fernandezarrojo – 3rd expert on this subject based on the ideXlab platform

  • biochemical characterization of a Beta Fructofuranosidase from rhodotorula dairenensis with transfructosylating activity
    Fems Yeast Research, 2009
    Co-Authors: Patricia Gutierrezalonso, Francisco J Plou, Lucia Fernandezarrojo, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Rhodotorula dairenensis was characterized biochemically. The enzyme molecular mass was estimated to be 680 kDa by analytical gel filtration and 172 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, of which the N-linked carbohydrate accounts for 16% of the total mass. It displays optimum activity at pH 5 and 55-60 degrees C. The enzyme shows broad substrate specificity, hydrolyzing sucrose, 1-kestose, nystose, leucrose, raffinose and inulin. Although the main reaction catalyzed by this enzyme is sucrose hydrolysis, it also exhibits transfructosylating activity that, unlike other microbial BetaFructofuranosidases, produces a varied type of prebiotic fructooligosaccharides containing Beta-(2–>1)- and Beta-(2–>6)-linked fructose oligomers. The maximum concentration of fructooligosaccharides was reached at 75% sucrose conversion and it was 87.9 g L(-1). The 17.0% (w/w) referred to the total amount of sugars in the reaction mixture. At this point, the amounts of 6-kestose, neokestose, 1-kestose and tetrasaccharides were 68.9, 10.6, 2.6 and 12.7 g L(-1), respectively.

  • molecular and biochemical characterization of a Beta Fructofuranosidase from xanthophyllomyces dendrorhous
    Applied and Environmental Microbiology, 2009
    Co-Authors: Dolores Linde, Isabel Macias, Lucia Fernandezarrojo, Francisco J Plou, Antonio J Jimenez, Maria Fernandezlobato

    Abstract:

    : An extracellular BetaFructofuranosidase from the yeast Xanthophyllomyces dendrorhous was characterized biochemically, molecularly, and phylogenetically. This enzyme is a glycoprotein with an estimated molecular mass of 160 kDa, of which the N-linked carbohydrate accounts for 60% of the total mass. It displays optimum activity at pH 5.0 to 6.5, and its thermophilicity (with maximum activity at 65 to 70 degrees C) and thermostability (with a T(50) in the range 66 to 71 degrees C) is higher than that exhibited by most yeast invertases. The enzyme was able to hydrolyze fructosyl-Beta-(2–>1)-linked carbohydrates such as sucrose, 1-kestose, or nystose, although its catalytic efficiency, defined by the k(cat)/K(m) ratio, indicates that it hydrolyzes sucrose approximately 4.2 times more efficiently than 1-kestose. Unlike other microbial BetaFructofuranosidases, the enzyme from X. dendrorhous produces neokestose as the main transglycosylation product, a potentially novel bifidogenic trisaccharide. Using a 41% (wt/vol) sucrose solution, the maximum fructooligosaccharide concentration reached was 65.9 g liter(-1). In addition, we isolated and sequenced the X. dendrorhous BetaFructofuranosidase gene (Xd-INV), showing that it encodes a putative mature polypeptide of 595 amino acids and that it shares significant identity with other fungal, yeast, and plant BetaFructofuranosidases, all members of family 32 of the glycosyl-hydrolases. We demonstrate that the Xd-INV could functionally complement the suc2 mutation of Saccharomyces cerevisiae and, finally, a structural model of the new enzyme based on the homologous invertase from Arabidopsis thaliana has also been obtained.