Cell Wall, Membrane, and Intracellular Peptidase Activities of Propionibacterium shermanii

Sahlstrøm, Stefan; Espinosa, Cruz; Langsrud, Thor; Sørhaug, T.

doi:10.3168/jds.s0022-0302(89)79115-3

Cited by 29 publications

(14 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Langsrud et al (1978b) established that propionibacteria also produced intracellular peptidases G Panon which were released by autolysis in hard cheeses. Sahlstrom et al (1989) found peptidase activities in cell wall, membrane and intracellular fractions of P shermanii. Perez Chaia et al (1990), studying the activity of peptidases belonging to propionibacteria, found a greater affinity for proline p-nitroanilide than for leucine p-nitroanilide.…”

Section: Introductionmentioning

confidence: 89%

Purification and characterization of a proline iminopeptidase from Propionibacterium shermanii 13673

Panon

1990

Lait

View full text Add to dashboard Cite

Summary -A proline lminopepndase activity was round in P shermanii 13673. The enzyme activity was present in the intracellular fraction. The peptidase was purifisd approximately 80 times by ionexchange chromatography on Fractogel T8K DEAE 650 and gel filtration on 8ephacryl 8-100 HR. The purified enzyme appeared as a single band after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It had a molecular weight of 61 000. Optima for activity of the.purified enzyme were 40 oC and pH 8.0. The enzymatic activity was inhibited by phenylmethylsulfonylfluoride (1 mM). Divalent ions Zn, Co, Cu and Fe alsohad an inhibitor}t effect. The peptidase hydrolyzed specifically Pro p-NA amino acid, dipeptides Pro-Met, Pro-Phe, Pro-Le, Pro-lieu, Pro-G1yand 13-casomorphin des-Tyr fragment 7.

show abstract

Section: Introductionmentioning

confidence: 89%

Purification and characterization of a proline iminopeptidase from Propionibacterium shermanii 13673

Panon

1990

Lait

View full text Add to dashboard Cite

show abstract

“…They are mainly intracellularly located [12,23,27,31]. Four of them identified in P. freudenreichii are supposed to play a major role in Swiss cheese flavor development: a proline iminopeptidase [25,27], prolinase and prolidase [29] and two phenylalanine aminopeptidases [10].…”

Section: Dairy Propionibacteriamentioning

confidence: 99%

Strain variability of the cell-free proteolytic activity of dairy propionibacteria towards β-casein peptides

Lemée

Gagnaire

Maubois

1998

Lait

View full text Add to dashboard Cite

-Strain selection of dairy propionibacteria is based on COz' acetate and propionate production. However, another criterion such as proteolytic activity could be of industrial interest for selection of flavor ripening agents. Given that the propionibacteria are variously able to autolyse and that proteolytic activity is mainly intracellularly located, the proteolytic potential was evaluated on the cell-free extracts of 37 dairy propionibacteria strains. The substrate used to detect proteolytic activity was a tryptic/chymotryptic hydrolysate of~-casein. The evaluation was performed at a temperature of 30 "C and pH of 5.7. The increase in the free NH z groups over a 24 h period was monitored as weil as the evolution of the reversed-phase chromatographie profiles. In addition, for 14 strains, the free amino acids released from the~-casein peptides were determined. Ali the strains were able to hydrolyze~-casein peptides. Difference of proteolytic activity was observed among and within the four dairy propionibacteria species. This variability was expressed more in terms of nature of the products released (peptides and free amino acids) than in terms of degree of proteolytic activity. From the results, a strain selection system may be developed using as substrate the tryptic/chymotryptic~-casein hydrolysate and as criteria the degree of hydrolysis at 24 h and the amount and the nature of free ami no acids released by cellfree ex tracts. Such a selection will give useful data for cheesemakers, especially if characterization of autolytic ability in the cheese environment is also determined. © InralElsevier, Paris.propionibacteria / proteolysis / peptide / Cree amino acid / selection Résumé -Souche dépendance de l'activité protéolytique intracellulaire de bactéries propioniques laitières sur un substrat laitier (hydrolysat de caséine~). La sélection des souches de bactéries propioniques est fondée sur la production de COz' d'acétate et de propionate. Cependant, un autre critère tel que l'activité protéolytique pourrait présenter un intérêt industriel afin de sélectionner des souches susceptibles de produire des précurseurs de flaveurs. En tenant compte du fait que les bactéries propioniques possèdent une capacité variable à s'autolyser et que * Correspondence and reprints. E-mail: gagnaire@labtechno.roazhon.inra.fr of intracellular peptidase activities in cheese curd during ripening requires evidently an autolytic mechanism induced in propionibacteria cells, either physiologically or by environmental conditions. Such an autolysis was recently observed under in vitro conditions [20, 21, 23, 24] and in Emmental (Valence F., personal communication). l'activité protéolytique est localisée principalement dans la fraction cytoplasmique de la bacté-rie, nous avons évalué le potentielprotéolytiqued'extrait intracellulairede 37 souchesde bactéries propioniques. Le substrat utilisé pour tester l'activité de manière globale était un hydrolysat trypsique/chymotrypsique de caséine~. L'hydrolyse était réalisée à 30 "C et à pH...

show abstract

“…How-ever, the low proteinase activity of propionibacteria, which have numerous peptidases (Flogerghagen et al, 1978;Sahlstrôm et al, 1989;El Soda et al, 1992), renders their growth in cheese dependent on the primary hydrolysis of casein by starter bacteria, micrococci of the contaminating milk flora (Ritter and Schwab, 1968) or, possibly, the proteolytic activity of rennet or plasmin.…”

Section: Introductionmentioning

confidence: 99%

Influence of casein proteolysis by starter bacteria, rennet and plasmin on the growth of propionibacteria in Swiss-type cheese

Baer

1995

Lait

View full text Add to dashboard Cite

Cell Wall, Membrane, and Intracellular Peptidase Activities of Propionibacterium shermanii

Cited by 29 publications

References 12 publications

Purification and characterization of a proline iminopeptidase from Propionibacterium shermanii 13673

Purification and characterization of a proline iminopeptidase from Propionibacterium shermanii 13673

Strain variability of the cell-free proteolytic activity of dairy propionibacteria towards β-casein peptides

Influence of casein proteolysis by starter bacteria, rennet and plasmin on the growth of propionibacteria in Swiss-type cheese

Contact Info

Product

Resources

About