Release of wine monoterpenes from natural precursors by glycosidases from Oenococcus oeni

Michlmayr, Herbert; Nauer, Stefan; Brandes, Walter; Schümann, Christina; Kulbe, Klaus D.; Hierro, Andrés M. del; Eder, Reinhard

doi:10.1016/j.foodchem.2012.04.099

Cited by 61 publications

(42 citation statements)

References 37 publications

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“…Four O. oeni isolates retained their enzymatic activity under the conditions of winemaking. In a similar study, cell-bound glucosidase and arabinosidase activities from O. oeni strains released high levels of monoterpenes from natural substrates under optimal conditions [42]. The enzymes showed broad substrate specificities (release of both primary and tertiary terpene alcohols) and remained active in grape juice.…”

Section: Glycosidasesmentioning

confidence: 77%

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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Section: Glycosidasesmentioning

confidence: 77%

Enzymes for Wine Fermentation: Current and Perspective Applications

Claus

Mojsov

2018

Fermentation

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“…Therefore, it seems to bear a certain irony that, in the context of enzymatic release of attractive wine aroma compounds from glycosylated precursors, we previously identified Lb. brevis as a versatile source of glycosidases (25,39,40).…”

Section: Discussionmentioning

confidence: 99%

Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

Michlmayr

Hell

Lorenz

et al. 2013

Appl Environ Microbiol

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Due to their potential prebiotic properties, arabinoxylan-derived oligosaccharides [(A)XOS] are of great interest as functional food and feed ingredients. While the (A)XOS metabolism of Bifidobacteriaceae has been extensively studied, information regarding lactic acid bacteria (LAB) is still limited in this context. The aim of the present study was to fill this important gap by characterizing candidate (A)XOS hydrolyzing glycoside hydrolases (GHs) identified in the genome of Lactobacillus brevis DSM 20054. Two putative GH family 43 xylosidases (XynB1 and XynB2) and a GH family 43 arabinofuranosidase (Abf3) were heterologously expressed and characterized. While the function of XynB1 remains unclear, XynB2 could efficiently hydrolyze xylooligosaccharides. Abf3 displayed high specific activity for arabinobiose but could not release arabinose from an (A)XOS preparation. However, two previously reported GH 51 arabinofuranosidases from Lb. brevis were able to specifically remove ␣-1,3-linked arabinofuranosyl residues from arabino-xylooligosaccharides (AXHm3 specificity). These results imply that Lb. brevis is at least genetically equipped with functional enzymes in order to hydrolyze the depolymerization products of (arabino)xylans and arabinans. The distribution of related genes in Lactobacillales genomes indicates that GH 43 and, especially, GH 51 glycosidase genes are rare among LAB and mainly occur in obligately heterofermentative Lactobacillus spp., Pediococcus spp., members of the Leuconostoc/Weissella branch, and Enterococcus spp. Apart from the prebiotic viewpoint, this information also adds new perspectives on the carbohydrate (i.e., pentose-oligomer) metabolism of LAB species involved in the fermentation of hemicellulose-containing substrates.

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“…and Pediococci spp. (Guilloux-Benatier et al 1993;Grimaldi et al 2000Grimaldi et al , 2005bMichlmayr et al 2012b). Interestingly, a previous study reported that βG of SD-2a and 31MBR is an intracellular form and 31MBR possesses higher intracellular activity than SD-2a (Li et al 2012b).…”

Section: Resultsmentioning

confidence: 98%

“…The βG activity of both strains decreasing sharply at 45°C may be due to the damage caused by high temperature to intact cells, since an optimum temperature of 50°C has been observed for crude βG of the two strains (Li et al 2012b). Usually, pH is known as an important factor to affect the enzyme activity, especially low pH is considered as an inhibitor of βG activity (Grimaldi et al 2000;Michlmayr et al 2010bMichlmayr et al , 2012b.…”

Section: Resultsmentioning

confidence: 99%

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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Release of wine monoterpenes from natural precursors by glycosidases from Oenococcus oeni

Cited by 61 publications

References 37 publications

Enzymes for Wine Fermentation: Current and Perspective Applications

Enzymes for Wine Fermentation: Current and Perspective Applications

Arabinoxylan Oligosaccharide Hydrolysis by Family 43 and 51 Glycosidases from Lactobacillus brevis DSM 20054

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

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