β-Glucoside metabolism in Oenococcus oeni: Cloning and characterisation of the phospho-β-glucosidase bglD

Capaldo, Angela; Walker, M.; Ford, C. M.; Jiranek, Vladimir

doi:10.1016/j.foodchem.2010.09.036

Cited by 21 publications

(30 citation statements)

References 39 publications

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“…Such properties are consistent with the reported characteristics of AscB from Pectobacterium carotovorum LY34. However, the noninhibition of the activity on this enzyme by Mn 2ϩ was different from the marked inhibition observed in the corresponding enzymes, AscB and BglD, from Oenococcus oeni (21,22). In addition, the recombinant protein showed good pH stability compared to other reported enzymes; it was markedly stable under a broad pH range, from pH 5 to 9, with little loss of activity after incubation for up to 24 h (data not shown).…”

Section: Discussionmentioning

confidence: 68%

“…In addition, the recombinant protein showed good pH stability compared to other reported enzymes; it was markedly stable under a broad pH range, from pH 5 to 9, with little loss of activity after incubation for up to 24 h (data not shown). Such properties are different from those of the 6-phospho-␤-glucosidase BglD, which showed the greatest activity at pH 5.0, with only 9% activity at pH 3.5 and 12% activity at pH 7.0 retained (22). This pH tolerance would be due to the alkaline environment from which Pbgl25-217 is derived.…”

Section: Discussionmentioning

confidence: 84%

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Characterization of a Novel Metagenome-Derived 6-Phospho-β-Glucosidase from Black Liquor Sediment

Yang

Niu

et al. 2013

Appl Environ Microbiol

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The enzyme 6-phospho-␤-glucosidase is an important member of the glycoside hydrolase family 1 (GH1). However, its catalytic mechanisms, especially the key residues determining substrate specificity and affinity, are poorly understood. A metagenomederived gene sequence, encoding a novel 6-phospho-␤-glucosidase designated Pbgl25-217, was isolated and characterized. The optimal conditions for enzymatic activity were 37°C and pH 7; Ca 2؉ , Mg 2؉ , and Mn 2؉ stabilized the activity of Pbgl25-217, whereas Ni 2؉ , Fe 2؉ , Zn 2؉ , Cu 2؉ , and Fe 3؉ inhibited its activity. The K m and V max of Pbgl25-217 were 4.8 mM and 1,987.0 U mg ؊1 , respectively. Seven conserved residues were recognized by multiple alignments and were tested by site-directed mutagenesis for their functions in substrate recognition and catalytic reaction. The results suggest that residues S427, Lys435, and Tyr437 act as "gatekeepers" in a phosphate-binding loop and play important roles in phosphate recognition. This functional identification may provide insights into the specificity of 6-phospho-␤-glycosidases in GH1 and be useful for designing further directed evolution.

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Section: Discussionmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 84%

Characterization of a Novel Metagenome-Derived 6-Phospho-β-Glucosidase from Black Liquor Sediment

Yang

Niu

et al. 2013

Appl Environ Microbiol

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“…PEP-PTS is a bacterial transport system that allows bacterial cells to grow on various carbon sources, including β-glucosides (Deutscher et al, 2006). Capaldo et al (2011) proposed that O. oeni was able to take up β-glucosides via a PEP-PTS involving phosphorylation and the subsequent hydrolysis of the phosphorylated glucosides in the cytoplasm through the action of phospho-β-glucosidases. The related genes bglA, B, C and D, encoding PEP-PTS components EIIC, EIIA, EIIB and phospho-β-glucosidase, have been studied (Capaldo et al, 2011).…”

Section: Figure 1amentioning

confidence: 99%

“…Capaldo et al (2011) proposed that O. oeni was able to take up β-glucosides via a PEP-PTS involving phosphorylation and the subsequent hydrolysis of the phosphorylated glucosides in the cytoplasm through the action of phospho-β-glucosidases. The related genes bglA, B, C and D, encoding PEP-PTS components EIIC, EIIA, EIIB and phospho-β-glucosidase, have been studied (Capaldo et al, 2011). Low enzyme activity of whole cells for 31MBR might be due to the lack of PEP-PTS.…”

Section: Figure 1amentioning

confidence: 99%

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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“…The difference could be attributed to the presence of the phosphoenolpyruvate dependent phosphotransferase system (PEP-PTS). Capaldo et al (2011) pointed out that O. oeni were able to take up β-glucosides via the PEP-PTS, which involves phosphorylation and subsequent hydrolysis of the phosphorylated glucosides through the action of phospho-β-glucosidases (Capaldo et al 2011). This could also well explain the results from other authors that intact cells of the bacteria showed high βG activity while low or no intracellular and extracellular activities were observed (McMahon et al 1999;Michlmayr et al 2010b).…”

Section: Resultsmentioning

confidence: 74%

Assessment of β-d-glucosidase activity of intact cells of two Oenococcus oeni strains with synthetic and natural substrates

Li¹,

Ma²,

Fan³

et al. 2016

Czech J. Food Sci.

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The β-d-glucosidase (βG) activity of intact cells of Oenococcus oeni SD-2a and 31MBR was assessed with synthetic and natural substrates, also its partial characterisation was investigated. Results showed that intact cells of both strains showed βG activity, SD-2a performing higher than 31MBR, against either synthetic or natural substrate. The high βG activity of SD-2a intact cells under wine-like temperature, pH, ethanol concentration, and glucose concentration could be of great interest for its utilisation in winemaking. SD-2a proved promising for aroma enrichment in winemaking.

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β-Glucoside metabolism in Oenococcus oeni: Cloning and characterisation of the phospho-β-glucosidase bglD

Cited by 21 publications

References 39 publications

Characterization of a Novel Metagenome-Derived 6-Phospho-β-Glucosidase from Black Liquor Sediment

Characterization of a Novel Metagenome-Derived 6-Phospho-β-Glucosidase from Black Liquor Sediment

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 of intact cells of two Oenococcus oeni strains with synthetic and natural substrates

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