A Novel β‐Glucosidase from <i>Sporidiobolus pararoseus</i>: Characterization and Application in Winemaking

Baffi, Milla Alves; Tobal, Thaise Mariá; Henrique, João; Lago, João Henrique G.; Leite, Rodrigo Simões Ribeiro; Boscolo, Maurício; Gomes, Eleni; Silva, Roberto da

doi:10.1111/j.1750-3841.2011.02293.x

Cited by 50 publications

(48 citation statements)

References 24 publications

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“…The β‐glucosidase activities studied in the 4 isolates showed a pH optimum of 6.0, similar to the results obtained in Sporiobolus pararoseus (Baffi and others ). Interestingly, the β‐glucosidase activity of H. uvarum was not affected in the pH range tested.…”

Section: Discussionsupporting

confidence: 88%

Screening of β‐Glucosidase and β‐Xylosidase Activities in Four Non‐Saccharomyces Yeast Isolates

López

Mateo

Maicas

2015

Journal of Food Science

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The finding of new isolates of non-Saccharomyces yeasts, showing beneficial enzymes (such as β-glucosidase and β-xylosidase), can contribute to the production of quality wines. In a selection and characterization program, we have studied 114 isolates of non-Saccharomyces yeasts. Four isolates were selected because of their both high β-glucosidase and β-xylosidase activities. The ribosomal D1/D2 regions were sequenced to identify them as Pichia membranifaciens Pm7, Hanseniaspora vineae Hv3, H. uvarum Hu8, and Wickerhamomyces anomalus Wa1. The induction process was optimized to be carried on YNB-medium supplemented with 4% xylan, inoculated with 106 cfu/mL and incubated 48 h at 28 °C without agitation. Most of the strains had a pH optimum of 5.0 to 6.0 for both the β-glucosidase and β-xylosidase activities. The effect of sugars was different for each isolate and activity. Each isolate showed a characteristic set of inhibition, enhancement or null effect for β-glucosidase and β-xylosidase. The volatile compounds liberated from wine incubated with each of the 4 yeasts were also studied, showing an overall terpene increase (1.1 to 1.3-folds) when wines were treated with non-Saccharomyces isolates. In detail, terpineol, 4-vinyl-phenol and 2-methoxy-4-vinylphenol increased after the addition of Hanseniaspora isolates. Wines treated with Hanseniaspora, Wickerhamomyces, or Pichia produced more 2-phenyl ethanol than those inoculated with other yeasts.

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Section: Discussionsupporting

confidence: 88%

Screening of β‐Glucosidase and β‐Xylosidase Activities in Four Non‐Saccharomyces Yeast Isolates

López

Mateo

Maicas

2015

Journal of Food Science

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“…The enzyme was tolerant to ethanol, showing tolerance up to 40% of ethanol (Table 2). Previous studies in literature reported cellulases and hemicellulases which are inhibited by ethanol (van DYK et al, 2010;BAFFI et al, 2011). In the present study, the enzyme remained 75% of residual activity at 40% of ethanol showing high tolerance to this compound.…”

Section: Resultssupporting

confidence: 56%

Substract and temperature effect on xylanase production by aspergillus fumigatus using low cost agricultural wastes

Gomes¹,

Santos²,

Franciscon³

et al. 2016

Biosci. J.

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This study reports the optimization of xylanase production under solid state fermentation (SSF) by a thermotolerant Aspergillus fumigatus strain (SCB4) isolated from sugarcane bagasse piles of Brazilian Cerrado. Different combinations of low-cost agricultural byproducts in SSF were evaluated: sugarcane bagasse and wheat bran (1:1), sugarcane bagasse and corn straw (1:1) and only sugarcane bagasse. The enzyme biosynthesis by SSF was carried out at different temperatures (40, 45, 50 and 55 o C). The maximum levels of xylanase activity were obtained after 24 h at 45 °C using a culture medium containing sugarcane bagasse and wheat bran (1:1). Under optimal conditions, the fungal culture produced 574 U g -1 of xylanase (units/g of dry substrate). The crude enzyme showed optimal activity at 60 °C and pH 4.5. It exhibited thermostability up to 55 °C, wide range of pH stability and tolerance to ethanol, xylose and glucose. The physicochemical properties shown by this enzyme are appropriate for its application in hydrolysis of lignocellulosic residues for ethanol production and other bioproducts.

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“…As β ‐glucosidases are usually inhibited by glucose, the sugar tolerance of WaExg2 is one of its outstanding features. Similar beneficial properties were reported for β ‐glucosidases produced by a few other yeast strains (Swangkeaw et al ., ; Baffi et al ., ). In addition to sugar tolerance, WaExg2 proved to be stable under various wine‐related conditions.…”

Section: Discussionmentioning

confidence: 97%

The yeastWickerhamomyces anomalusAS1 secretes a multifunctional exo-β-1,3-glucanase with implications for winemaking

Schwentke

Sabel

Petri

et al. 2014

Yeast

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A multifunctional exo-β-1,3-glucanase (WaExg2) was purified from the culture supernatant of the yeast Wickerhamomyces anomalus AS1. The enzyme was identified by mass spectroscopic analysis of tryptic peptide fragments and the encoding gene WaEXG2 was sequenced. The latter codes for a protein of 427 amino acids, beginning with a probable signal peptide (17 aa) for secretion. The mature protein has a molecular mass of 47 456 Da with a calculated pI of 4.84. The somewhat higher mass of the protein in SDS-PAGE might be due to bound carbohydrates. Presumptive disulphide bridges confer a high compactness to the molecule. This explains the apparent smaller molecular mass (35 kDa) of the native enzyme determined by electrophoresis, whereas the unfolded form is consistent with the theoretical mass. Enzymatic hydrolysis of selected glycosides and glycans by WaExg2 was proved by TLC analysis of cleavage products. Glucose was detected as the sole hydrolysis product from laminarin, underlining that the enzyme acts as an exoglucanase. In addition, the enzyme efficiently hydrolysed small β-linked glycosides (arbutin, esculin, polydatin, salicin) and disaccharides (cellobiose, gentiobiose). WaExg2 was active under typical wine-related conditions, such as low pH (3.5-4.0), high sugar concentrations (up to 20% w/v), high ethanol concentrations (10-15% v/v), presence of sulphites (up to 2 mM) and various cations. Therefore, the characterized enzyme might have multiple uses in winemaking, to increase concentrations of sensory and bioactive compounds by splitting glycosylated precursors or to reduce viscosity by hydrolysis of glycan slimes.

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A Novel β‐Glucosidase from Sporidiobolus pararoseus: Characterization and Application in Winemaking

Cited by 50 publications

References 24 publications

Screening of β‐Glucosidase and β‐Xylosidase Activities in Four Non‐Saccharomyces Yeast Isolates

Screening of β‐Glucosidase and β‐Xylosidase Activities in Four Non‐Saccharomyces Yeast Isolates

Substract and temperature effect on xylanase production by aspergillus fumigatus using low cost agricultural wastes

The yeastWickerhamomyces anomalusAS1 secretes a multifunctional exo-β-1,3-glucanase with implications for winemaking

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