A novel extracellular β-glucosidase from Issatchenkia terricola: Isolation, immobilization and application for aroma enhancement of white Muscat wine

González-Pombo, Paula; Fariña, Laura; Carrau, Francisco; Batista‐Viera, Francisco; Brena, Beatríz M.

doi:10.1016/j.procbio.2010.07.016

Cited by 106 publications

(64 citation statements)

References 30 publications

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“…10a, the immobilized β-glucosidase retained about 73% of its initial activity after 6 weeks of storage, whereas the free β-glucosidase lost more than 80% of its initial activity. These results indicated that the immobilization with magnetic nanoparticles improved the stability of β-glucosidase, and similar results have been reported for other immobilization methods (Fan et al 2011;González-Pombo et al 2011;Su et al 2010).…”

Section: Storage Stability and Reusabilitysupporting

confidence: 88%

Immobilization of β-glucosidase onto Magnetic Nanoparticles and Evaluation of the Enzymatic Properties

et al. 2013

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This paper reports on a novel and efficient β-glucosidase immobilization method using magnetic Fe 3 O 4 nanoparticles as a carrier. Based on response surface methodology, the optimal immobilization conditions obtained were: glutaraldehyde (GA) concentration, 0.20%; enzyme concentration, 50.25 μg/mL; cross-linking time, 2.21 h; and the maximum activity recovery reached 89.35%. The magnetic immobilized enzyme was characterized by Fourier transform infrared spectroscopy (FTIR), transmission electron microscope (TEM), and vibrating sample magnetometer (VSM). FTIR revealed that β-glucosidase was successfully immobilized on the magnetic nanoparticles. TEM showed that enzyme-magnetic nanoparticles possessed nano-scale size distribution. VSM confirmed that the enzyme-magnetic nanoparticles were superparamagnetic. The properties of the immobilized β-glucosidase were improved, and the immobilized β-glucosidase exhibited wider pH and temperature ranges of activation, higher accessibility of the substrate, better thermal stability, and better storage stability than that of the free enzyme. The enzyme-magnetic nanoparticles could be separated magnetically for easy reuse. Immobilization of β-glucosidase onto the magnetic nanoparticles has the potential for industrial application.

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Section: Storage Stability and Reusabilitysupporting

confidence: 88%

Immobilization of β-glucosidase onto Magnetic Nanoparticles and Evaluation of the Enzymatic Properties

et al. 2013

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“…Glycosidase activities have been also detected in various non-Saccharomyces yeasts (Candida, Hanseniaspora, Pichia, Metschnikowia, Rhodotorula, Trichosporon, Wickerhamomyces) [43][44][45][46][47][48][49][50][51][52] (Table 5). Several experiments on the technical application of yeast glycosidases to improve organoleptic quality of wines gave positive results [40,44,46,49,50].…”

Section: Glycosidasesmentioning

confidence: 99%

“…Several experiments on the technical application of yeast glycosidases to improve organoleptic quality of wines gave positive results [40,44,46,49,50].…”

Section: Glycosidasesmentioning

confidence: 99%

Enzymes for Wine Fermentation: Current and Perspective Applications

Claus

Mojsov

2018

Fermentation

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Enzymes are used in modern wine technology for various biotransformation reactions from prefermentation through fermentation, post-fermentation and wine aging. Industrial enzymes offer quantitative benefits (increased juice yields), qualitative benefits (improved color extraction and flavor enhancement) and processing advantages (shorter maceration, settling and filtration time). This study gives an overview about key enzymes used in winemaking and the effects of commercial enzyme preparations on process engineering and the quality of the final product. In addition, we highlight on the presence and perspectives of beneficial enzymes in wine-related yeasts and lactic acid bacteria.

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“…After the actions of endoglucanase and cellobiohydrolase, β-glucosidase (Bgl) removes glucose from either non-reducing cellobiose or cellotriose (Wu et al 2013). Because of its contribution to the hydrolysis of cellulose, Bgl has attracted significant attention for use in a wide range of industrial processes, such as improving the flavor of wine and clarifying juice in beverage and food production (Ketudat Cairns and Esen 2010;González-Pombo et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

Long¹,

Shi²,

Li³

et al. 2016

BioResources

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A 56-kDa β-glucosidase (TthBgl) derived from Thermotoga thermarum DSM 5069 was expressed and purified from Escherichia coli BL21 (DE3). The purified enzyme showed hydrolytic activity towards only pnitrophenyl-β-D-glucopyranoside among the synthetic glycosides tested. The pH maximum was 5.0, and under the conditions tested, maximal activity was at 85 ºC, and pH stability occurred from 5.0 to 6.0. After being incubated at 80 ºC for 120 min, TthBgl retained 80% of its original activity. The β-glucosidase had no apparent requirement for metal ions or other co-factors, but its activity was significantly inhibited by 0.1% SDS and 1mM Cu 2+ , in which only 3% and 10% residual activity was maintained, respectively. The Vmax of TthBgl was 8.79 U mg -1 for pnitrophenyl-β-D-glucopyranoside, while the Km was 2.41 mM. The Enzyme activity was gradually inhibited by the addition of glucose, but remained approximately 50% of its original value in 500 mM glucose. 789.25 mg/L glucose was released from cellobiose by the incubation of 0.2 U/mL TthBgl for 9 h at 75 ºC. According to a phylogenetic analysis, TthBgl belongs to the glycosyl hydrolase family 3 (GH3).

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A novel extracellular β-glucosidase from Issatchenkia terricola: Isolation, immobilization and application for aroma enhancement of white Muscat wine

Cited by 106 publications

References 30 publications

Immobilization of β-glucosidase onto Magnetic Nanoparticles and Evaluation of the Enzymatic Properties

Immobilization of β-glucosidase onto Magnetic Nanoparticles and Evaluation of the Enzymatic Properties

Enzymes for Wine Fermentation: Current and Perspective Applications

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

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