One-step purification and characterization of an intracellular β-glucosidase from Metschnikowia pulcherrima

González-Pombo, Paula; Pérez, Gabriel; Carrau, Francisco; Guisán, José M.; Batista‐Viera, Francisco; Brena, Beatríz M.

doi:10.1007/s10529-008-9708-3

Cited by 53 publications

(35 citation statements)

References 15 publications

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“…This is coincident with previous reports that ethanol at concentrations of 4%, 8% and 10% led to an enhancement of βG activity, while enzyme activity decreased sharply at even higher concentrations Barbagallo et al, 2004aBarbagallo et al, , 2004bGrimaldi et al, 2005b;González-Pombo et al, 2008). The enhancement behaviour of ethanol at low concentrations could be ascribed to the glycosyl transferase activity of βG (Pemberton et al, 1980;Barbagallo et al, 2004b).…”

Section: Figure 1asupporting

confidence: 91%

“…1B) of the enzyme decreased at pH 3.5 compared with that at pH 5.0. This could be explained by previous reports that the optimum pH of βG was around 5.0 (Spagna et al, 1998;Barbagallo et al, 2004a;González-Pombo et al, 2008;Michlmayr et al, 2010a), notwithstanding that an optimum pH of 3.8 has also been reported (Grimaldi et al, 2005b). In addition, at a winelike pH of 3.5, whole cells of strain SD-2a had the highest activity under temperatures of 30, 40 and 50°C (Fig.…”

Section: Enzyme Characterisations Under Different Conditionssupporting

confidence: 52%

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Assessment of β-D-Glucosidase Activity from Two Typical Strains of the Lactic Acid Bacteria, Oenococcus oeni, in China

Fan

Zhang

et al. 2016

SAJEV

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β-D-glucosidase (βG) is one of the most interesting glycosidases for the hydrolysis of glycoconjugated precursors to release active aromatic compounds in musts and wines. Oenococcus oeni strains SD-2a and 31MBR are widely used in Chinese wines to reduce the acidity. In the present study, the βG activity of the two strains was localised and partially characterised using synthetic substrate. The activity occurred in whole cells, sonication supernatants and debris, but not in the culture supernatants for both strains. Whole cells of strain SD-2a possessed greater βG activity, while strain 31MBR showed higher enzyme activity in the sonication supernatants. Strain 31MBR exhibited higher total enzyme activity than strain SD-2a. The optimum temperatures for βG from the two strains were 40ºС at pH 3.5 and 50ºС at pH 5.0, respectively. Ethanol at low concentrations had a positive effect on βG activity in both strains, while a wine-like pH (3.5) decreased the enzyme activity to a great extent. Whole cells of strain SD-2a showed the highest activity among all samples tested under wine-like conditions. Thus, strain SD-2a proved to have potential for aroma improvement in winemaking.

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Section: Figure 1asupporting

confidence: 91%

Section: Enzyme Characterisations Under Different Conditionssupporting

confidence: 52%

Assessment of β-D-Glucosidase Activity from Two Typical Strains of the Lactic Acid Bacteria, Oenococcus oeni, in China

Fan

Zhang

et al. 2016

SAJEV

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“…In fact, during crushing, oleuropein, demethyloleuropein and ligstroside present in the fruit are hydrolysed by action of endogenous b-glucosidases leading to the formation of secoiridoids aglycons such as 3,4-DHPEA-EDA, p-HPEA-EDA, ligstroside aglycone ( p-HPEA-EA) and 3,4-DHPEA-EA [2,[78][79][80]. It is admitted that mechanical crushers are more effective in the extraction of phenolic compounds than traditional stone mills [81].…”

Section: Technological Factorsmentioning

confidence: 99%

Hydrophilic antioxidants of virgin olive oil. Part 2: Biosynthesis and biotransformation of phenolic compounds in virgin olive oil as affected by agronomic and processing factors

Riachy

Priego‐Capote

León

et al. 2011

Eur. J. Lipid Sci. Technol.

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The biosynthesis of the phenolic fraction of olive fruits during ripening and the transformations occurring in this moiety during virgin olive oil (VOO) extraction are discussed in this paper. The influence of agronomical factors that can significantly affect the phenolic profile of VOO is also discussed. Particularly, it is worth emphasizing the role of genetic factors, cultivation and climatic conditions such as water availability, atmospheric temperature, altitude, health status of the fruits, alternate bearing in the olive, and some processing factors such as crushing, malaxation time and temperature or volume of water added during milling. Among these parameters, special attention has been paid to genetic factors due to the high variability observed among Olea europaea genotypes for all recorded traits. In this context, interesting experimental results have been obtained with cultivated and wild olive trees, and also with segregating populations resulting from olive breeding programs. To the authors' knowledge, reviews evaluating the influence of the main factors that contribute to the profile of hydrophilic phenols have not been previously published. The discussion concerning olive breeding programs is a major and novel aspect to be emphasized considering recent trends to obtain new olive cultivars that confer better organoleptic properties and better quality to VOO.

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“…4). Similarly, β-glucosidase from X. regalis, Lycoperdon pyriforme, A. niger, Metschnikowia pulcherrima, exhibited the maximum activity at pH 5.0 and the least activity at pH 9.0 and 4.0 [20,33,34,35] . Purified form of β-glucosidases of Volvareilla volvacea displayed a broad pH optimum between 6.2 to 7.4 for β-glucosidase I and 5.4 -6.6 for β-glucosidase II [36] .…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of β-Glucosidase fromAspergillus niger

Narasimha¹,

Sridevi²,

Ramanjaneyulu³

et al. 2015

International Journal of Food Properties

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Aspergillus niger, an isolate of soil contaminated with effluents from cotton ginning mill was grown in Czapek-Dox medium containing sawdust, Triton-X 100 and urea for production of an extracellular β-glucosidase. β-Glucosidase enzyme was purified (86-fold) from culture filtrate of A. niger by employing ammonium sulphate precipitation and gel filtration on sephadex G -75. The molecular mass of the purified enzyme was estimated to be 95 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The enzyme had an optimal activity on p-nitrophenyl β-D glucoside (PNPBG) at 50°C and pH 5.0. The K m and Vmax of the enzyme on PNPBG at 50°C and pH 5 were 8.0 mM and 166 µmol/min/mg of protein, respectively. The enzyme could hydrolyze cellobiose and lactose but not sucrose. Heavy metals like Hg 2+ , Al 3+ and Ag + inhibited the activity whereas Zn 2+ and detergents such as Triton-X 100 A c c e p t e d M a n u s c r i p t 2 and Tween-80 increased the activity at 0.01%. The enzyme activity increased in the presence of methanol and ethanol.

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One-step purification and characterization of an intracellular β-glucosidase from Metschnikowia pulcherrima

Cited by 53 publications

References 15 publications

Assessment of β-D-Glucosidase Activity from Two Typical Strains of the Lactic Acid Bacteria, Oenococcus oeni, in China

Assessment of β-D-Glucosidase Activity from Two Typical Strains of the Lactic Acid Bacteria, Oenococcus oeni, in China

Hydrophilic antioxidants of virgin olive oil. Part 2: Biosynthesis and biotransformation of phenolic compounds in virgin olive oil as affected by agronomic and processing factors

Purification and Characterization of β-Glucosidase fromAspergillus niger

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