A beta-glucosidase gene isolated from wine Lactobacillus plantarum is regulated by abiotic stresses

Spano, Giuseppe; Rinaldi, Alessandra; Ugliano, Maurizio; Moio, Luigi; Beneduce, Luciano; Massa, Salvatore

doi:10.1111/j.1365-2672.2004.02521.x

Cited by 81 publications

(69 citation statements)

References 23 publications

(25 reference statements)

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“…Some Lactobacillus species have also displayed the ability to survive the harsh wine conditions (G-Alegría et al, 2004;Pozo-Bayón et al, 2005), of which the species Lactobacillus plantarum has shown the most potential as a starter culture (for review see Du and a commercial culture has recently been released by Lallemand as Lactobacillus plantarum V22 ® (Bou & Krieger, 2004;Fumi et al, 2010). This species of Lactobacillus also shows a more diverse enzymatic profile than O. oeni (Matthews et al, 2004;Spano et al, 2005;Mtshali et al, 2010), which could play an important role in the modification of the wine aroma profile (Guerzoni et al, 1995;Swiegers et al, 2005;Matthews et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Lerm¹,

Engelbrecht²,

Toit³

2016

SAJEV

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This study focused on characterising 23 Oenococcus oeni and 19 Lactobacillus plantarum strains isolated from the South African wine environment for the development of potential commercial malolactic fermentation (MLF) starter cultures. These strains were characterised with regards to oenological important characteristics, including the genetic screening for enzyme-encoding genes (enzymes that are involved/implicated in wine aroma modification, as well as enzymes pertaining to the wholesomeness of the final wine product), their fermentation capabilities, the ability to maintain viability during MLF, as well as the volatile acidity production. A total of three O. oeni and three L. plantarum strains were selected at the completion of this study. These six strains showed the most potential during the characterisation stages of the study and were able to successfully complete MLF in Pinotage wine. It was also found that L. plantarum strains displayed a more diverse enzyme profile than O. oeni strains, particularly with regards to the presence of the aroma-modifying enzymes β-glucosidase and phenolic acid decarboxylase (PAD), which implies the future use of this species in the modification of the wine aroma profile and use as commercial starter culture.

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Section: Introductionmentioning

confidence: 99%

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Lerm¹,

Engelbrecht²,

Toit³

2016

SAJEV

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“…rhamnosidases. Based on their adaptation to the harsh wine milieu and their general hydrolytic abilities toward different glycosides (16,17,50), wine-related lactic acid bacteria (LAB) have attracted much interest as a potential source of novel glycosidases (34).Consequently, several (intracellular) glycosidases from different wine-related bacterial species have already been identified and characterized (11,12,(36)(37)(38)48). Another driving force for the identification and characterization of bacterial glycosidases, including rhamnosidases, is the observation that plant secondary metabolites (i.e., flavonoids) with potential health benefits have improved bioavailability in their aglycon forms (26).…”

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confidence: 99%

“…Consequently, several (intracellular) glycosidases from different wine-related bacterial species have already been identified and characterized (11,12,(36)(37)(38)48). Another driving force for the identification and characterization of bacterial glycosidases, including rhamnosidases, is the observation that plant secondary metabolites (i.e., flavonoids) with potential health benefits have improved bioavailability in their aglycon forms (26).…”

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confidence: 99%

Characterization of Two Distinct Glycosyl Hydrolase Family 78 α- l -Rhamnosidases from Pediococcus acidilactici

Michlmayr

Brandes

Eder

et al. 2011

Appl Environ Microbiol

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␣-L-Rhamnosidases play an important role in the hydrolysis of glycosylated aroma compounds (especially terpenes) from wine. Although several authors have demonstrated the enological importance of fungal rhamnosidases, the information on bacterial enzymes in this context is still limited. In order to fill this important gap, two putative rhamnosidase genes (ram and ram2) from Pediococcus acidilactici DSM 20284 were heterologously expressed, and the respective gene products were characterized. In combination with a bacterial ␤-glucosidase, both enzymes released the monoterpenes linalool and cis-linalool oxide from a muscat wine extract under ideal conditions. Additionally, Ram could release significant amounts of geraniol and citronellol/ nerol. Nevertheless, the potential enological value of these enzymes is limited by the strong negative effects of acidity and ethanol on the activities of Ram and Ram2. Therefore, a direct application in winemaking seems unlikely. Although both enzymes are members of the same glycosyl hydrolase family (GH 78), our results clearly suggest the distinct functionalities of Ram and Ram2, probably representing two subclasses within GH 78: Ram could efficiently hydrolyze only the synthetic substrate p-nitrophenyl-␣-L-rhamnopyranoside (V max ‫؍‬ 243 U mg ؊1 ). In contrast, Ram2 displayed considerable specificity toward hesperidin (V max ‫؍‬ 34 U mg ؊1 ) and, especially, rutinose (V max ‫؍‬ 1,200 U mg ؊1 ), a disaccharide composed of glucose and rhamnose. Both enzymes were unable to hydrolyze the flavanone glycoside naringin. Interestingly, both enzymes displayed indications of positive substrate cooperativity. This study presents detailed kinetic data on two novel rhamnosidases, which could be relevant for the further study of bacterial glycosidases.␣-L-Rhamnosidases (EC 3.2.1.40) catalyze the hydrolysis of a wide spectrum of natural glycosides containing terminal Lrhamnose. The biotechnological interest in rhamnosidases includes the debittering of citrus fruit juices (naringinase and hesperidinase), the release of flavonoids from rhamnosylated precursors, and the production of L-rhamnose as starting material for chemical synthesis (52). Further, rhamnosidases may play a crucial role in wine making due to their contributions to releasing grape-derived aroma compounds (mainly terpenes and terpenic alcohols). Depending on the grape variety, rutinosides (␣-L-rhamnopyranosyl-␤-D-glucopyranoside) constitute 6 to 13% of the terpenic glycosides found in wine (29). The combination of ␤-D-glucosidase and ␣-L-rhamnosidase allows the sequential release of volatile compounds from these precursors (18). Several authors (9, 32, 46) have demonstrated the enological value of fungal (Aspergillus sp.) rhamnosidases. Based on their adaptation to the harsh wine milieu and their general hydrolytic abilities toward different glycosides (16,17,50), wine-related lactic acid bacteria (LAB) have attracted much interest as a potential source of novel glycosidases (34).Consequently, several (intracellular) glycosid...

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“…βG activity in O. oeni, the main bacterial species conducting MLF, was confirmed more than 20 years ago (Guilloux-Benatier et al, 1993). Over the past decades, numerous investigations have been conducted, providing evidence for the potential βG activity of O. oeni strains for flavor enhancement in wines (Spano et al, 2005;Michlmayr et al, 2010;Gagné et al, 2011). It has been reported that the possession of glycosidic activities is widespread and strain dependent among O. oeni strains (Barbagallo et al, 2004;Grimaldi et al, 2005;Saguir et al, 2009).…”

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Identification and Localization of β-D-Glucosidase from Two Typical Oenococcus oeni Strains

Huang

et al. 2016

Polish Journal of Microbiology

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A b s t r a c t β-D-glucosidase (βG) gene from Oenococcus oeni SD-2a and 31MBR was cloned, sequenced and analyzed, also intracellular βG of the two strains was further localized. The results showed that βG gene of the two strains was in high homology (> 99%) to reported βG gene, confirming both strains possess βG activity at the molecular level. Intracellular βG of SD-2a is a mainly soluble protein, existing mostly in the cytoplasm and to some extent in the periplasm. While for 31MBR, intracellular βG is mainly insoluble protein existing in the cytoplasmic membrane. This study provides basic information for further study of the metabolic mechanism of βG from O. oeni SD-2a and 31MBR. 210was cloned, sequenced and analyzed through bioinformatics, also the intracellular βG of the two strains was further localized.O. oeni strains SD-2a and 31MBR, stored in our laboratory, were cultivated as described before (Li et al., 2012a). Bacterial growth was monitored by measuring the OD 600 nm until the mid-log phase (about 40 h and 20 h for SD-2a and 31MBR respectively). Genomic DNA was extracted with Genomic DNA isolation Kit (TaKaRa, Shiga, Japan) as recommended by the manufacturer and verified on a 1% (w/v) agarose gel. Primers 5'TTGTCTAAGATTACTT CAATTATT TCA 3' and 5' TTAACTTTGATTGGCGA GTTTA3' , deduced from the nucleotide sequences of βG gene previously identified in O. oeni PSU-1 (Makarova et al., 2006), were used. For the PCR experiments, 25 ng of genomic DNA isolated from O. oeni SD-2a or 31MBR was added to a 25 μl PCR mixture containing 0.5 U of ExTaq polymerase, 0.2 mM of dNTP mix, 1 × PCR buffer (TaKaRa, Shiga, Japan), and 0.25 mM of each primer. The reaction was carried out at the following temperature profile: 94°C, 4 min; 94°C, 1 min; 58°C, 40 s; 72°C, 1.5 min -35 cycles (using the icycler PCR Bio-Rad). The PCR reaction was terminated at 72°C for 10 min. PCR fragments were analysed on gel electrophoresis by applying 5 μl of sample to 1.0% agarose gel and a 2000 bp ladder (TaKaRa, Shiga, Japan) was used as the standard marker. The amplified fragments were purified with PCR Clean-up Kit (TaKaRa, Shiga, Japan), connected with vector PMD18-T (TaKaRa, Shiga, Japan), and transformed into Escherichia coli DH5α. Plasmid was extracted using Plasmid Extraction Kit (TaKaRa, Shiga, Japan) and sequenced by Takara Biotechnology Co., Ltd. Dalian, China.The alignment of the deduced protein sequences against that of O. oeni PSU-1 was carried out with software Clustalx 1.81. Physical and chemical parameters of deduced amino acid sequences were computed with ProtParam (Gasteiger et al., 2005). The amino acid scale of hydropathicity was defined following the ProtScale (Gasteiger et al., 2005). Transmembrane helices were predicted with TMHMM Server v. 2.0 (http://www. cbs.dtu.dk/services/TMH MM-2.0/). The presence and location of signal peptide cleavage sites in amino acid sequence was predicted with SignalP 4.0 server (http://www.cbs.dtu.dk/services/SignalP/). Finally, the subcellular localization prediction was conducted with PSO...

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A beta-glucosidase gene isolated from wine Lactobacillus plantarum is regulated by abiotic stresses

Cited by 81 publications

References 23 publications

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Characterization of Two Distinct Glycosyl Hydrolase Family 78 α- l -Rhamnosidases from Pediococcus acidilactici

Identification and Localization of β-D-Glucosidase from Two Typical Oenococcus oeni Strains

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