Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Aguiar‐Oliveira, Elizama; Maugeri, Francisco

doi:10.1590/s0104-66322011000300002

Cited by 27 publications

(34 citation statements)

References 24 publications

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“…LEB-V10 yeast and verified a loss of activity up to 61ºC. They suggest that the enzyme instability at higher temperatures led to the loss of transfructosylation capacity (Aguiar-Oliveira & Maugeri, 2011). …”

Section: Effect Of Ph and Temperature On Fructooligosaccharide Producmentioning

confidence: 82%

<b>Screening of whole yeast free-cells and optimization of pH and temperature for fructooligosaccharides production

Deffert

Agustini

Picheth

et al. 2017

Acta Sci. Biol. Sci.

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ABSTRACT. Fructooligosaccharides are catalyzed by β-fructofuranosidase enzyme, produced by many microorganisms. However, in order to achieve a more profitable, low time-consuming process with lower cost, researchers have sought alternatives. This study aimed to select and identify yeasts able to produce fructooligosaccharides and evaluate the influence of pH and temperature on their synthesis. Yeast suspensions, solutions of 500 g L -1sucrose and three values of pH (4.5, 5.5, and 6.5) and temperature (40, 50, and 60ºC) were tested. Yeast species were identified by molecular techniques. Among 141 yeast isolates from grapes, 65 were able to synthesize fructooligosaccharides. The maximum concentration of fructooligosaccharides was 4.8% (w v -1 ), and Saccharomyces cerevisiae 222 produced 1-kestose and nystose.

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Section: Effect Of Ph and Temperature On Fructooligosaccharide Producmentioning

confidence: 82%

<b>Screening of whole yeast free-cells and optimization of pH and temperature for fructooligosaccharides production

Deffert

Agustini

Picheth

et al. 2017

Acta Sci. Biol. Sci.

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“…Based on the methodologies described and employed in previous studies (Hernalsteens and Maugeri ; Aguiar‐Oliveira and Maugeri ), Rhodotorula sp. LEB‐V10 was cultivated in a medium containing sugar cane molasses and corn steep liquor.…”

Section: Methodsmentioning

confidence: 99%

“…The standard conditions for FOS synthesis from commercial sucrose were based on previous works (Hernalsteens and Maugeri ; Aguiar‐Oliveira and Maugeri ): 50% (w/v) of sucrose in sodium acetate buffer (50 mM) at pH 4.5 or 6.0, 50C and 6 U i /mL. For comparison, syntheses were performed with the standard immobilized enzyme (without any additions to the dispersion medium) under the same standard conditions.…”

Section: Methodsmentioning

confidence: 99%

“…An extracellular fructosyltransferase (FTase; EC 2.4.1.9) from Rhodotorula sp. LEB‐V10 partially purified in free and immobilized forms has presented interesting results regarding its catalytic characteristics (Hernalsteens and Maugeri ; Aguiar‐Oliveira and Maugeri ; Alvarado‐Huallanco and Maugeri ). After isolation of the yeast Rhodotorula sp.…”

Section: Introductionmentioning

confidence: 99%

“…In previous studies (Aguiar‐Oliveira and Maugeri, , ), it is possible to find important information about alternatives for immobilization of FTase in niobium (Nb) such as random or oriented immobilization and enzymatic adsorption in the presence of different concentrations of substrate (sucrose) and stabilizing salt (CuSO 4 ). However, the effect of these immobilization methods on the enzymatic catalytic ability had not yet been assessed.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effects of the Addition of Substrate and Salts in Both the Fructosyltransferase Immobilization and Its Catalytic Properties

Aguiar‐Oliveira

Maugeri

2012

Journal of Food Biochemistry

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The partially purified extracellular fructosyltransferase from Rhodotorula sp. LEB-V10 immobilized in niobium particles in the presence of 4 and 8% (w/v) of sucrose showed no differences concerning fructooligosaccharide (FOS) synthesis, concluding that the enzymatic active sites are not related to immobilization. When immobilized in the presence of 5 and 10 mM CuSO4, this enzyme presented a slight increase in FOS yield (9-12%). In addition, no FOS molecule was produced when the synthesis was conducted with 10 mM CuSO4. This result might suggest that, besides the strong stabilization, the interaction between salt and enzyme should result in a "safer" conformational structure for the enzymatic active sites. FOS synthesis was also affected by the presence of 10 mM MnCl2 or NaCl, but only in a small scale than with CuSO4. PRACTICAL APPLICATIONSThe fructosyltransferase (FTase) from Rhodotorula sp. immobilized in niobium has proven to be a promising biocatalyst for fructooligosaccharide (FOS) production, a prebiotic sugar. Adsorption, a technique for FTase immobilization, presents several advantages, but it can, unfortunately, provide a biocatalyst with lower enzymatic activity depending on how the enzyme is linked to the support particles. Exploring the possibility of increasing FOS production by adding compounds such as sucrose (substrate) or CuSO4 (capable of promoting stability) during the process of adsorption has a great importance because it permits one to evaluate the interactions between enzyme and compound. Furthermore, the addition of salts (also capable of increasing stability) into the reactive medium for FOS production is also important to evaluate in order to understand if stability and higher yields are possible to be achieved together.

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