Hydrolysis of muscle myofibrillar proteins by Lactobacillus curvatus and Lactobacillus sake

Sanz, Yolanda; Fadda, Silvina; Vignolo, Graciela; Aristoy, M‐Concepción; Oliver, G.; Toldrá, Fidel

doi:10.1016/s0168-1605(99)00134-8

Cited by 99 publications

(54 citation statements)

References 28 publications

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“…The Bifidobacterium and Lactobacillus genera, which were applied in the present technological process conditions, require certain amino acids for their development, i.e. arginine, isoleucine, leucine, tyrosine, cysteine and valine (Fadda et al, 1999;Sanz et al, 1999aSanz et al, , 1999b. The results obtained here showed that these were present in the product as free amino acids or in peptides of low molecular weight.…”

Section: Discussionmentioning

confidence: 61%

Effect of probiotic bacteria on antiradical activity of peptides isolated from dry-cured loins

Okoń

Stadnik

Dolatowski

2017

CyTA - Journal of Food

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The aim of the study was to evaluate the effect of probiotic bacteria strains (Lactobacillus rhamnosus LOCK900 and Bifidobacterium animalis ssp. lactis BB12) on antiradical activity of peptides isolated from dry-cured loins after fermentation and 4 months cold storage followed by in vitro gastrointestinal digestion. Studies have shown that the use of probiotic bacteria for the manufacture of dry-cured products affects the formation of protein proteolysis products with antiradical activity during cold storage and gastrointestinal enzyme digestion. Loins with the B. animalis ssp. lactis strain BB12 were characterised by the highest antiradical peptide activity among products after fermentation and cold storage (1.85 mg Trolox/mg peptides; 2.8 mg Trolox/mg peptides) than loins with a mixture of strains (1.17 mg Trolox/mg peptides; 3.36 mg Trolox/mg peptides).Efecto de las bacterias probióticas en la actividad antiradical de péptidos aisladas de lomo curado en seco RESUMEN El objetivo de este estudio fue evaluar el efecto de cepas de bacteria probiótica (Lactobacillus rhamnosus LOCK900 y Bifidobacterium animalis ssp. lactis BB12) en la actividad antiradical de péptidos aisladas de lomo curado en seco después de una fermentación y almacenamiento en frío de 4 meses seguidos de digestión gastrointestinal in vitro. Algunos estudios han mostrado que el uso de bacteria probiótica para la elaboración de productos curados en seco afecta a la formación de productos de proteólisis proteínica con actividad antiradical durante el almacenamiento en frío y la digestión enzimática gastrointestinal. El lomo con cepa BB12 de Bifidobacterium animalis ssp. lactis se caracterizó por tener la mayor actividad de péptidos antiradicales entre los productos que habían estado fermentados y almacenados en frío (1,85 mg de Trolox/mg péptidos; 2,8 mg de Trolox/mg péptidos) por encima del lomo con mezcla de cepas (1,17 mg de Trolox/mg péptidos; 3,36 mg de Trolox/mg péptidos).

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Section: Discussionmentioning

confidence: 61%

Effect of probiotic bacteria on antiradical activity of peptides isolated from dry-cured loins

Okoń

Stadnik

Dolatowski

2017

CyTA - Journal of Food

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“…The cell extract used for purification was obtained by lysozyme and ultrasonic treatments as previously described (6,26). The aminopeptidase was purified as described below.…”

Section: Methodsmentioning

confidence: 99%

“…Several meat-derived Lactobacillus spp. have shown proteolytic activity on sarcoplasmic and myofibrillar proteins, and L. sakei in particular has been demonstrated to play an important potential role in amino acid generation (6,7,26). Thus, fundamental biochemical research has been focused on intracellular peptidases of L. sakei, and a number of peptidases have been purified (20,22,24,27).…”

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confidence: 99%

Purification and Characterization of an Arginine Aminopeptidase from Lactobacillus sakei

Sanz

Toldrá

2002

Appl Environ Microbiol

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An arginine aminopeptidase (EC 3.4.11.6) that exclusively hydrolyzes basic amino acids from the amino (N) termini of peptide substrates has been purified from Lactobacillus sakei. The purification procedure consisted of ammonium sulfate fractionation and three chromatographic steps, which included hydrophobic interaction, gel filtration, and anion-exchange chromatography. This procedure resulted in a recovery rate of 4.2% and a 500-fold increase in specific activity. The aminopeptidase appeared to be a trimeric enzyme with a molecular mass of 180 kDa. The activity was optimal at pH 5.0 and 37°C. The enzyme was inhibited by sulfhydryl group reagents and several divalent cations (Cu 2؉ , Hg 2؉ , and Zn 2؉ ) but was activated by reducing agents, metalchelating agents, and sodium chloride. The enzyme showed a preference for arginine at the N termini of aminoacyl derivatives and peptides. The K m values for Arg-7-amido-4-methylcoumarin (AMC) and Lys-AMC were 15.9 and 26.0 M, respectively. The nature of the amino acid residue at the C terminus of dipeptides has an effect on hydrolysis rates. The activity was maximal toward dipeptides with Arg, Lys, or Ala as the C-terminal residue. The properties of the purified enzyme, its potential function in the release of arginine, and its further metabolism are discussed because, as a whole, it could constitute a survival mechanism for L. sakei in the meat environment.

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“…It has been shown that several Lactobacillus spp. exhibit proteolytic activity on porcine muscle myofibrillar and sarcoplasmic proteins (7,8,28). These studies highlighted the potential role of L. sakei in amino acid and peptide generation especially from sarcoplasmic proteins.…”

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confidence: 97%

Purification and Characterization of an X-Prolyl-Dipeptidyl Peptidase from Lactobacillus sakei

Sanz

Toldrá

2001

Appl Environ Microbiol

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An X-prolyl-dipeptidyl peptidase has been purified from Lactobacillus sakei by ammonium sulfate fractionation and five chromatographic steps, which included hydrophobic interaction, anion-exchange chromatography, and gel filtration chromatography. This procedure resulted in a recovery yield of 7% and an increase in specificity of 737-fold. The enzyme appeared to be a dimer with a subunit molecular mass of approximately 88 kDa. Optimal activity was shown at pH 7.5 and 55°C. The enzyme was inhibited by serine proteinase inhibitors and several divalent cations (Cu 2؉ , Hg 2؉ , and Zn 2؉). The enzyme almost exclusively hydrolyzed X-Pro from the N terminus of each peptide as well as fluorescent and colorimetric substrates; it also hydrolyzed X-Ala at the N terminus, albeit at lower rates. K m s for Gly-Pro-and Lys-Ala-7-amido-4-methylcoumarin were 29 and 88 M, respectively; those for Gly-Pro-and Ala-Pro-p-nitroanilide were 192 and 50 M, respectively. Among peptides, ␤-casomorphin 1-3 was hydrolyzed at the highest rates, while the relative hydrolysis of the other tested peptides was only 1 to 12%. The potential role of the purified enzyme in the proteolytic pathway by catalyzing the hydrolysis of peptide bonds involving proline is discussed.Lactic acid bacteria constitute one of the most important group of microorganisms used in food fermentation. In the last decades, the metabolic traits of these bacteria have been the object of exhaustive studies, which evidence promising applications (12). The proteolytic properties of dairy lactic acid bacteria are among the best characterized to date (5, 13). This is a consequence of the impact of proteolysis on the physiology of these organisms as well as on the development of texture and flavor of dairy products (6, 18). Proteolysis on milk proteins is initiated by a cell wall-associated proteinase, which hydrolyzes caseins into oligopeptides. The generated peptides are mainly translocated via the oligopeptide transport system and, further, hydrolyzed by a pool of intracellular peptidases, which include endopeptidases, aminopeptidases, dipeptidases, tripeptidases, and dipeptidyl peptidases (13).Lactobacillus sakei is the most competitive species in meat fermentation and therefore constitutes a frequently used starter culture. The proteolytic events that occur during meat processing also lead to the generation of small peptides and free amino acids, which are considered to be flavor compounds (1, 31). In fermented meat products, muscle as well as microbial enzymes are responsible for the proteolytic changes, but their roles remain elusive (21, 31). Particularly, the studies on the proteolytic system of meat lactobacilli are rather limited. It has been shown that several Lactobacillus spp. exhibit proteolytic activity on porcine muscle myofibrillar and sarcoplasmic proteins (7,8,28). These studies highlighted the potential role of L. sakei in amino acid and peptide generation especially from sarcoplasmic proteins. Attention has also been focused on intracellular peptidases of L. ...

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Hydrolysis of muscle myofibrillar proteins by Lactobacillus curvatus and Lactobacillus sake

Cited by 99 publications

References 28 publications

Effect of probiotic bacteria on antiradical activity of peptides isolated from dry-cured loins

Effect of probiotic bacteria on antiradical activity of peptides isolated from dry-cured loins

Purification and Characterization of an Arginine Aminopeptidase from Lactobacillus sakei

Purification and Characterization of an X-Prolyl-Dipeptidyl Peptidase from Lactobacillus sakei

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