Peptidase activities in debittering and nondebittering strains of lactobacilli

Abboudi, M. El; Soda, M. El; Pandian, S.; Barreau, M.; Trépanier, G.; Simard, R.E.

doi:10.1016/0958-6946(92)90044-m

Cited by 29 publications

(24 citation statements)

References 20 publications

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“…However, the effect of homogenization was found more significant for PTA-SN values. Similar result was obtained by El Abboudi et al (1990) for homogenized Lactobacillus casei ssp. casei in Cheddar cheese, which did not increase gross proteolysis as measured by TCA-SN, but accelerated the breakdown of peptides (El Soda & Pandian 1991).…”

Section: Resultssupporting

confidence: 88%

The effect of low pressure-homogenized lactic cultures on the development of proteolysis in cheese slurry

Çoşkun

2005

World J Microbiol Biotechnol

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The aim of this study was to determine the effect of low pressure-homogenization of lactic acid bacteria (LAB) on the development of proteolysis in the slurry medium. For the slurry, the milk was pasteurized at 65°C for 30 min, cooled to 32°C and coagulated. The curd obtained was blended; the dry matter was adjusted to 30% by adding distilled water, placed into the flasks and autoclaved. The LAB Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. cremoris, Lactobacillus delbrueckii subsp. bulgaricus, Streptococcus thermophilus, and Lactobacillus helveticus were used in cheese slurry. Homogenization was performed at 30 MPa and 40°C. The cheese slurries were incubated with and without homogenized cultures at 9 and 30°C for up to 72 h. During incubation, the changes in trichloroacetic acid-soluble nitrogen (TCA-SN) and phosphotungstic acid-soluble nitrogen (PTA-SN) as well as pH were monitored. The results showed that pH development was slower in the slurries to which homogenized culture was added. Higher TCA-SN and PTA-SN values were obtained from the slurries incubated at 30°C. Moreover, higher TCA-SN and PTA-SN values were found in the slurries incubated with homogenized mesophilic culture and Lb. helveticus (P<0.05). The results suggested that homogenization of the cultures was a promising method for the acceleration of cheese ripening.

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Section: Resultssupporting

confidence: 88%

The effect of low pressure-homogenized lactic cultures on the development of proteolysis in cheese slurry

Çoşkun

2005

World J Microbiol Biotechnol

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“…This carboxypeptidase is not able to remove a proline in the Cterminal position, which suggests that no carboxypeptidase P is synthesized by these species. The presence of a carboxypeptidase has been reported for Lactobacillus casei (8,9) and L. helveticus (36), but this point was controversial because of the synthetic substrate used. Carboxypeptidase activity was also recently suspected from the identification of peptides in Emmentaler juice at the end of the ripening (26).…”

Section: Discussionmentioning

confidence: 99%

Hydrolysis of Sequenced β-Casein Peptides Provides New Insight into Peptidase Activity from Thermophilic Lactic Acid Bacteria and Highlights Intrinsic Resistance of Phosphopeptides

Deutsch

Mollé

Gagnaire

et al. 2000

Appl Environ Microbiol

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The peptidases of thermophilic lactic acid bacteria have a key role in the proteolysis of Swiss cheeses during warm room ripening. To compare their peptidase activities toward a dairy substrate, a tryptic/chymotryptic hydrolysate of purified ␤-casein was used. Thirty-four peptides from 3 to 35 amino acids, including three phosphorylated peptides, constitute the ␤-casein hydrolysate, as shown by tandem mass spectrometry. Cell extracts prepared from Lactobacillus helveticus ITG LH1, ITG LH77, and CNRZ 32, Lactobacillus delbrueckii subsp. lactis ITG LL14 and ITG LL51, L. delbrueckii subsp. bulgaricus CNRZ 397 and NCDO 1489, and Streptococcus thermophilus CNRZ 385, CIP 102303, and TA 060 were standardized in protein. The peptidase activities were assessed with the ␤-casein hydrolysate as the substrate at pH 5.5 and 24°C (conditions of warm room ripening) by (i) free amino acid release, (ii) reverse-phase chromatography, and (iii) identification of undigested peptides by mass spectrometry. Regardless of strain, L. helveticus was the most efficient in hydrolyzing ␤-casein peptides. Interestingly, cell extracts of S. thermophilus were not able to release a significant level of free proline from the ␤-casein hydrolysate, which was consistent with the identification of numerous dipeptides containing proline. With the three lactic acid bacteria tested, the phosphorylated peptides remained undigested or weakly hydrolyzed indicating their high intrinsic resistance to peptidase activities. Finally, several sets of peptides differing by a single amino acid in a C-terminal position revealed the presence of at least one carboxypeptidase in the cell extracts of these species. Thermophilic lactobacilli such as Lactobacillus helveticus orLactobacillus delbrueckii along with Streptococcus thermophilus constitute essential lactic starters in Swiss-type cheese (400,000 tons of Emmentaler produced per year worldwide). The three species have a key role in the acidification step and in cheese proteolysis (13). Adequate proteolysis is essential for acceptable quality of the ripened cheese. Whole caseins are first hydrolyzed by milk protease (plasmin) and/or rennet (chymosin and pepsin) into large and intermediate-sized peptides. The proteinases and peptidases from starters subsequently hydrolyze them in small peptides and amino acids, which are known to be aroma precursors. In the three species considered, peptidases are intracellular enzymes released upon lysis in the curd, where they remain active for several weeks (14,40,41). Because of their predominant role in proteolysis, studies on peptidases of thermophilic lactobacilli and S. thermophilus have expanded greatly in recent years (5,18,35,36). Several aminopeptidases, dipeptidases, and peptidases specific to proline-containing peptides (prolidase, prolinase, X-prolyldipeptidyl aminopeptidase, and prolyl aminopeptidase) were isolated, cloned, and sequenced (20); only the general aminopeptidase(s) and the X-prolyl-dipeptidyl-aminopeptidase of thermophilic lactobacilli were shown to be...

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“…This enzyme pathway, which comprises proteinases, endopeptidases and exopeptidases, plays an important role in decreasing ripening time, in the acceleration of flavor development and in the reduction of bitterness (El Abboudi et al, 1992;Fortina, Nicastro, Carminati, Neviani, & Manachini, 1998;Fox, 1989).…”

Section: Introductionmentioning

confidence: 99%

Multilocus restriction typing: A tool for studying molecular diversity within Lactobacillus helveticus of dairy origin

Borgo

Ricci

Manachini

et al. 2007

International Dairy Journal

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Peptidase activities in debittering and nondebittering strains of lactobacilli

Cited by 29 publications

References 20 publications

The effect of low pressure-homogenized lactic cultures on the development of proteolysis in cheese slurry

The effect of low pressure-homogenized lactic cultures on the development of proteolysis in cheese slurry

Hydrolysis of Sequenced β-Casein Peptides Provides New Insight into Peptidase Activity from Thermophilic Lactic Acid Bacteria and Highlights Intrinsic Resistance of Phosphopeptides

Multilocus restriction typing: A tool for studying molecular diversity within Lactobacillus helveticus of dairy origin

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