Formation of methional by Lactococcus lactis IFPL730 under cheese model conditions

Amárita, Félix; Martínez-Cuesta, M. Carmen; Taborda, Gonzálo; Soto-Yarritu, P. López; Requena, Teresa; Peláez, Carmen

doi:10.1007/s00217-001-0420-y

“…Since the presence of C6 aldehydes may be associated with fish odor [32], this can be considered an undesired aromatic notes, especially in certain food preparations, such as those of dairy products; thus, fermentation could provide a valuable improvement of in aromatic profile of the sample. Methional was found in both of the UV-treated fermented samples, suggesting, as already suggested by other studies [74,75], that this aldehyde is produced by LAB. This compound was also previously isolated from Rhodomonas, another microalgae [71].…”

Section: Figure 3 Heat Map Performed On Volatile Chemical Classes' Concentrations Detected In Sterilized (St) or Uv-treated (Uv)supporting

confidence: 83%

Solid-State Fermentation of Arthrospira platensis to Implement New Food Products: Evaluation of Stabilization Treatments and Bacterial Growth on the Volatile Fraction

Martelli

¹

,

Cirlini

²

,

Neviani

³

et al. 2020

Foods

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Arthrospira platensis is a cyanobacterium widely used in food formulation and mainly consumed as a food supplement because of its high amount of proteins, vitamins and minerals. Different probiotic food supplements are present in the market, and a lactic acid fermented food product like dried spirulina could be useful not only to introduce lactic acid bacteria (LAB) with beneficial effects to the diet of consumers, but also to improve or change the aromatic profile of the substrate. Therefore, the aim of this study was the evaluation of lactic acid fermentation of A. platensis biomass, focusing on the consequent changes in the aromatic profile. For this purpose, two different stabilization treatments (UV light treatment and sterilization) were applied prior to fermentation with two LAB strains, Lacticaseibacillus casei 2240 and Lacticaseibacillus rhamnosus GG. The biomass proved to be a suitable matrix for solid-state fermentation, showing a LAB growth of more than 2 log CFU/g in 48 h. The fermentation process was also useful for off-flavor reduction. In particular, the fermentation process significantly influenced the concentration of those compounds responsible for aldehydic/ethereal, buttery/waxy (acetoin and diacetyl), alkane and fermented aromatic notes (isoamyl alcohol). The heat treatment of the matrix, in addition to guaranteed safety for consumers, led to an improved aroma after fermentation. In conclusion, a fermented spirulina powder with a different aromatic profile was obtained with the applied heat treatment. Fermentation with lactic acid bacteria can be an interesting tool to obtain cyanobacterial biomasses with more pleasant sensory properties for potential use in food formulations.

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“…In the work by Amárita et al [24] it was shown that the enzyme involved in the a-keto acid decarboxylase activity from L. lactis IFPL730 shows preference for branched-chain a-keto acids rather than methionine. In later work we demonstrated the ability of this strain to produce methional and the derived 3-methylthiopropanol in cheese slurries added with resting cells and the intracellular fraction of this bacterium [27]. We have also demonstrated enhancement of 2-methylbutanal formation by L. lactis IFPL730 in cheese when used as starter a lactococcal strain producing the bacteriocin lacticin 3147 [28].…”

Section: Introductionmentioning

confidence: 78%

Biochemical and molecular characterization of ?-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by

Delaplaza¹,

Fernandezdepalencia²,

Peláez³

et al. 2004

FEMS Microbiology Letters

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In this paper, we report for the first time on the identification, purification, and characterization of the alpha-ketoisovalerate decarboxylase from Lactococcus lactis, a novel enzyme responsible for the decarboxylation into aldehydes of alpha-keto acids derived from amino acid transamination. The kivd gene consisted of a 1647 bp open reading frame encoding a putative peptide of 61 kDa. Analysis of the deduced amino acid sequence indicated that the enzyme is a non-oxidative thiamin diphosphate (ThDP)-dependent alpha-keto acid decarboxylase included in the pyruvate decarboxylase group of enzymes. The active enzyme is a homo-tetramer that showed optimum activity at 45 degrees C and at pH 6.5 and exhibited an inhibition pattern typical for metal-dependant enzymes. In addition to Mg(2+), activity was observed in presence of other divalent cations such as Ca(2+), Co(2+) and Mn(2+). The enzyme showed the highest specific activity (80.7 Umg(-1)) for alpha-ketoisovalerate, an intermediate metabolite in valine and leucine biosynthesis. On the other side, decarboxylation of indole-3-pyruvate and pyruvate only could be detected by a 100-fold increase in the enzyme concentration present in the reaction.

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“…In the work by Amárita et al [24] it was shown that the enzyme involved in the α‐keto acid decarboxylase activity from L. lactis IFPL730 shows preference for branched‐chain α‐keto acids rather than methionine. In later work we demonstrated the ability of this strain to produce methional and the derived 3‐methylthiopropanol in cheese slurries added with resting cells and the intracellular fraction of this bacterium [27]. We have also demonstrated enhancement of 2‐methylbutanal formation by L. lactis IFPL730 in cheese when used as starter a lactococcal strain producing the bacteriocin lacticin 3147 [28].…”

Section: Introductionmentioning

confidence: 78%

Biochemical and molecular characterization of Î±-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids byLactococcus lactis

Plaza

¹

,

Palencia

²

,

Peláez

³

et al. 2004

FEMS Microbiology Letters

Self Cite

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In this paper, we report for the first time on the identification, purification, and characterization of the alpha-ketoisovalerate decarboxylase from Lactococcus lactis, a novel enzyme responsible for the decarboxylation into aldehydes of alpha-keto acids derived from amino acid transamination. The kivd gene consisted of a 1647 bp open reading frame encoding a putative peptide of 61 kDa. Analysis of the deduced amino acid sequence indicated that the enzyme is a non-oxidative thiamin diphosphate (ThDP)-dependent alpha-keto acid decarboxylase included in the pyruvate decarboxylase group of enzymes. The active enzyme is a homo-tetramer that showed optimum activity at 45 degrees C and at pH 6.5 and exhibited an inhibition pattern typical for metal-dependant enzymes. In addition to Mg(2+), activity was observed in presence of other divalent cations such as Ca(2+), Co(2+) and Mn(2+). The enzyme showed the highest specific activity (80.7 Umg(-1)) for alpha-ketoisovalerate, an intermediate metabolite in valine and leucine biosynthesis. On the other side, decarboxylation of indole-3-pyruvate and pyruvate only could be detected by a 100-fold increase in the enzyme concentration present in the reaction.

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Formation of methional by Lactococcus lactis IFPL730 under cheese model conditions

Cited by 15 publications

References 1 publication

Solid-State Fermentation of Arthrospira platensis to Implement New Food Products: Evaluation of Stabilization Treatments and Bacterial Growth on the Volatile Fraction

Solid-State Fermentation of Arthrospira platensis to Implement New Food Products: Evaluation of Stabilization Treatments and Bacterial Growth on the Volatile Fraction

Biochemical and molecular characterization of ?-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by

Biochemical and molecular characterization of Î±-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids byLactococcus lactis

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