2008
DOI: 10.1007/s10930-008-9154-z
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Influence of Polyols on the Stability and Kinetic Parameters of Invertase from Candida utilis: Correlation with the Conformational Stability and Activity

Abstract: Invertase (beta-D -fructofuranoside fructohydrolase-E.C. 3.2.1.26) is a sucrose hydrolyzing enzyme found in microbial, plant and animal sources. Invertase from Candida utilis is a dimeric glycoprotein composed of two identical monomer subunits with an apparent molecular mass of 150 kDa. We investigated the mechanism of stabilization of invertase with polyols (glycerol, xylitol, and sorbitol). Activity, thermodynamic and kinetic measurements of invertase were performed as a function of polyol concentration and … Show more

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Cited by 23 publications
(24 citation statements)
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“…With high catalytic activity in a wide range of temperature and pH (Chavez et al, 1997, Belcarz et al, 2002), the invertase serves not only for signal transduction from binding non-glucose targets into glucose signals, but also provides the necessary signal amplification through enzymatic turnovers, since most of the analyte are present in concentrations much below the working range of BGM and the enzymatic turnovers can amplify a low concentration of targets (picomolar or below) into high concentrations (in millimolar) of glucose. Yeast invertase has been used most frequently to develop BGM assays due to their high enzymatic activity ( k cat = 1540 s −1 and k cat / K m = 7390 at optimal condition), heat stability (active up to 80 °C, optimal between 60 – 75 °C), wide pH tolerance (pH 3 – 6, optimal at pH 5.5) and substrate specificity (sucrose, K m = 12.5 mM; and raffinose normally found in plants, K m = 150 mM)(Chavez et al, 1997, Gangadhara et al, 2008). …”
Section: Design Of the Bgm-based Biosensors For Ivds Of Non-glucosmentioning
confidence: 99%
“…With high catalytic activity in a wide range of temperature and pH (Chavez et al, 1997, Belcarz et al, 2002), the invertase serves not only for signal transduction from binding non-glucose targets into glucose signals, but also provides the necessary signal amplification through enzymatic turnovers, since most of the analyte are present in concentrations much below the working range of BGM and the enzymatic turnovers can amplify a low concentration of targets (picomolar or below) into high concentrations (in millimolar) of glucose. Yeast invertase has been used most frequently to develop BGM assays due to their high enzymatic activity ( k cat = 1540 s −1 and k cat / K m = 7390 at optimal condition), heat stability (active up to 80 °C, optimal between 60 – 75 °C), wide pH tolerance (pH 3 – 6, optimal at pH 5.5) and substrate specificity (sucrose, K m = 12.5 mM; and raffinose normally found in plants, K m = 150 mM)(Chavez et al, 1997, Gangadhara et al, 2008). …”
Section: Design Of the Bgm-based Biosensors For Ivds Of Non-glucosmentioning
confidence: 99%
“…In general, the effect of changes in temperature on the rates of enzyme-catalyzed reactions does not provide much information on the mechanism of biocatalysts. However, these effects can be important in indicating structural changes in enzyme [10,37].…”
Section: Effect Of Ph and Temperature On Activitymentioning
confidence: 99%
“…According to this model, in a protein-water-glycerol system, the glycerol is preferentially excluded from the immediate proximity of the protein (unfavourable interaction), and the protein will tend to be preferentially hydrated. 19 Thus, it will stabilize the protein native structure and prevent its denaturation; consequently the enzymatic activity can be maintained. 20 As we know that glycerol can penetrate the cell wall and the cytoplasmic membrane, 21 the same protein-stabilizing action can be occurring with alcohol dehydrogenases from A. terreus and R. oryzae.…”
Section: Resultsmentioning
confidence: 99%