Proteolytic activity of lactobacilli in a model goats' milk curd system

Parra, L.; Requena, Teresa; Casal, V.; Gómez, Rosario

doi:10.1111/j.1472-765x.1996.tb01340.x

Cited by 20 publications

(9 citation statements)

References 13 publications

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“…This activity was tentatively associated with the cell wall, since no hydrolytic change was detected in the protein patterns obtained when only CE were added. These results are comparable to those of Parra et al (24), who did not report any signif-icant increase in proteolysis when CE were added to a model involving goat's milk curds. In fact, most dairy lactic acid bacteria possess a single extracellular proteinase which initiates the hydrolysis of caseins into oligopeptides (14).…”

Section: Discussionsupporting

confidence: 89%

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

Fadda

Sanz

Vignolo

et al. 1999

Appl Environ Microbiol

120

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Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening, L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.

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Section: Discussionsupporting

confidence: 89%

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

Fadda

Sanz

Vignolo

et al. 1999

Appl Environ Microbiol

120

View full text Add to dashboard Cite

show abstract

“…The extracellular proteinase activities of both studied species seemed to have similar specificities for this substrate, although the hydrolysis caused by L. sake appeared to be also due to other intracellular enzymes. Moreover, the study of Parra et al (22) did not reveal increases in proteolysis when activities from the CE of lactobacilli were incorporated into a model goat's milk curds.…”

Section: Discussionmentioning

confidence: 92%

Hydrolysis of Pork Muscle Sarcoplasmic Proteins by Lactobacillus curvatus and Lactobacillus sake

Fadda

Sanz

Vignolo³

et al. 1999

Appl Environ Microbiol

135

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Lactobacillus curvatus CECT 904 and Lactobacillus sake CECT 4808 were selected on the basis of their proteolytic activities against synthetic substrates. Further, the effects of whole cells, cell extracts, and a combination of both enzymatic sources on muscle sarcoplasmic proteins were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography analyses. Strains of both species displayed proteinase activities on five sarcoplasmic proteins. The inoculation of whole cells caused a degradation of peptides, whereas the addition of cell extracts resulted in the generation of both hydrophilic and hydrophobic peptides. This phenomenon was remarkably more pronounced when L. curvatus was involved. Whole cells also consumed a great amount of free amino acids, while the addition of intracellular enzymes contributed to their generation. L. sake accounted for a greater release of free amino acids. In general, cell viability and also proteolytic events were promoted when cell suspensions were provided with cell extracts as an extra source of enzymes.

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“…casei strain was lower than that of 2 strains of Lb. plantarum, but this feature is strain-dependent (Parra et al, 1996;Oneca et al, 2007).…”

Section: Levels Of Faamentioning

confidence: 99%

Two strains of nonstarter lactobacilli increased the production of flavor compounds in soft cheeses

Milesi

Wolf

Bergamini

et al. 2010

Journal of Dairy Science

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The contribution to flavor generation and secondary proteolysis of 2 strains of mesophilic lactobacilli isolated from cheese was studied. Miniature soft cheeses (200 g) were produced with or without the inclusion of a culture of Lactobacillus plantarum I91 or Lactobacillus casei I90 in the starter composed of Streptococcus thermophilus. During ripening, cheeses containing the added lactobacilli showed an increased content of total free amino acids, but this increase was only significant in cheeses with Lb. plantarum I91. In addition, free amino acid profiles were modified by selective increases of some amino acids, such as Asp, Ser, Arg, Leu, and Phe. Cheeses inoculated with Lb. plantarum I91 or Lb. casei I90 were also characterized by a significantly higher concentration of diacetyl, a key flavor compound, and an increased content of acetoin. Results suggest an increase in the catabolism of either citrate or aspartate, with the production of the derived aroma compounds. Overall, aspartate content increased in both lactobacilli-added cheeses, whereas citrate was more or less constant, suggesting that aspartate could be the source of increased diacetyl and acetoin. A triangle aroma test showed that the addition of the lactobacilli strains significantly changed the sensory attributes of cheeses. At least 11 of 12 panelists commented that the aroma of cheeses with adjuncts was more buttery than that of control cheeses, which is desirable in most soft cheeses. Both Lb. plantarum I91 and Lb. casei I90 performed well as adjunct cultures by influencing cheese aroma development and cheese proteolysis.

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Proteolytic activity of lactobacilli in a model goats' milk curd system

Cited by 20 publications

References 13 publications

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

Hydrolysis of Pork Muscle Sarcoplasmic Proteins by Lactobacillus curvatus and Lactobacillus sake

Two strains of nonstarter lactobacilli increased the production of flavor compounds in soft cheeses

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