Maître de Conférences
Faculté des Sciences et Technologies - Nancy
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Microorganisms, 9 (11), pp. 2380.
Awussi, A. A., Roux, É., Humeau, C., Hafeez, Z., Maigret, B., Chang, O.K., Lecomte, X., Humbert, G., Miclo, L., Genay, M., Perrin, C., Dary-Mourot, A.
Growth of the lactic acid bacterium Streptococcus thermophilus in milk depends on its capacity to hydrolyze proteins of this medium through its surface proteolytic activity. Thus, strains exhibiting the cell envelope proteinase (CEP) PrtS are able to grow in milk at high cellular density. Due to its LPNTG motif, which is possibly the substrate of the sortase A (SrtA), PrtS is anchored to the cell wall in most S. thermophilus strains. Conversely, a soluble extracellular PrtS activity has been reported in the strain 4F44. It corresponds, in fact, to a certain proportion of PrtS that is not anchored to the cell wall but rather is released in the growth medium. The main difference between PrtS of strain 4F44 (PrtS4F44) and other PrtS concerns the absence of a 32-residue imperfect duplication in the prodomain of the CEP, postulated as being required for the maturation and correct subsequent anchoring of PrtS. In fact, both mature (without the prodomain at the N-terminal extremity) and immature (with the prodomain) forms are found in the soluble PrtS4F44 form along with an intact LPNTG at their C-terminal extremity. Investigations we present in this work show that (i) the imperfect duplication is not implied in PrtS maturation; (ii) the maturase PrtM is irrelevant in PrtS maturation which is probably automaturated; and (iii) SrtA allows for the PrtS anchoring in S. thermophilus but the SrtA of strain 4F44 (SrtA4F44) displays an altered activity.
International Dairy Journal, 56, pp. 159-168.
El Hatmi, H., Jrad, Z., Khorchani, T., Jardin, J., Poirson, C., Perrin, C., Cakir-Kiefer, C., Girardet, J.-M.
Camel milk was fermented by Streptococcus thermophilus LMD-9 strain, the proteolytic system of which yielded peptides from the milk proteins. The peptides were isolated by cation-exchange chromatography and ultrafiltration, and then separated into 9 fractions by reversed-phase high-performance liquid chromatography. Two fractions displayed efficient radical-scavenging properties shown by Trolox equivalent antioxidant capacity assay. At least 347 peptides distributed in the different fractions were identified by tandem mass spectrometry. They mainly derived from the four different caseins, glycosylation-dependent cell adhesion molecule-1 (GlyCAM-1), also called lactophorin, and peptidoglycan recognition protein-1. For the first time, cleavage sites were identified for these six proteins and the susceptibility of GlyCAM-1 towards bacterial proteolysis directly in milk was shown. Investigation of peptide sequences homologous to known bioactive peptides highlighted not less than 16 different putative biological activities. Fermentation of camel milk was thus a means of food processing to produce potential bioactive peptides.
Dairy Science and Technology, 96, pp. 623-636.
Galia, W., Jameh, N., Perrin, C., Genay, M., Dary, A.
The acquisition of prtS by Streptococcus thermophilus strains allowed hydrolysis
of caseins into peptides and then to increase their growth in milk. This leads to faster
milk acidification, which is important in dairy industry. However, some strains harboring
the same allele of prtS present different acidification rates, which could be explained by a
difference in the regulation of prtS expression.We chose two strains with the same allele
of prtS (including the same promoter region): one, PB302, is with high acidification rate
while the other, PB18O, is without. They exhibited similar growth in M17, but not in
milk, where PB302 showed better growth. The expression of prtS and activity of PrtS
were lower in PB18O, in the two media tested.We demonstrated that other genes known
to be involved in carbon and nitrogen metabolism were overexpressed in PB302.
Interestingly, these genes were overexpressed in milk compared to M17. Nearly all these
genes possessed a putative CodY-box in their promoter region. Taken together, difference
of gene expression detected in PB302 between milk (low-peptide medium) and
M17 (rich-peptide medium) and presence of a putative CodY-box is a feature of the
transcriptional pattern of CodY-regulated genes. Altogether, our results propose that
acquisition of prtS is not enough in certain strains to achieve rapid milk acidification.
High transcriptional level of dtpT, amiF, ilvC, ilvB, bcaT, livJ, ackA, codY, and prtS in fast
acidifying strain suggests that this transcriptional pattern could be required for fast milk
acidification in Streptococcus thermophilus.
Food Research International, 86, pp. 34-45.
Jameh, N., Galia, W., Awussi, A. A., Roux, É., Genay, M., Perrin, C., Dary, A.
In silico analysis of the genome of Streptococcus thermophilus LMD-9 revealed that this strain has a potential new peptide/nickel ABC transporter. We named this system OTS for Oligopeptide Transporter of S. thermophilus. It is composed of a peptide/nickel binding protein OtsA, two permeases OtsB and OtsC and a double ATPase OtsD. This system was presumably acquired by horizontal transfer from Actinobacteria or distant species like Lactococcus raffinolactis or Enterococcus asini may be via an intermediate like Lactococcus lactis or its ancestor. RT-PCR experiments proved that OTS gene cluster is transcribed and that at least the otsB, otsC, and otsD genes constitute an operon. A mutant LMD-9?ots, partially deleted for the otsA and otsB genes was constructed. Growth of LMD-9 and LMD-9?ots strains was monitored in the presence of different nitrogen sources and in the presence of urea and nickel. Results revealed that OTS is not implicated in nickel transport, but constitutes a new characterized transporter of peptides of small size, possibly di- and tripeptides in S. thermophilus.
LWT - Food Science and Technology, 70 (1), pp. 78-87.
Junjua, M., Kechaou, N., Chain, F., Awussi, A. A., Roussel, Y., Perrin, C., Roux, É., Langella, P., Bermúdez-Humarán, L.G., Le Roux, Y., Chatel, J.-M., Dary, A.
In spite of its contribution to health benefits of yogurt, probiotic properties of Streptococcus thermophilus remain less explored. Hence, we evaluated the capacities of 30 strains of different origins, to resist the stresses prevailing in digestive tracts, of adhering to the mucus producing HT29-MTX cells, as well as their anti-inflammatory properties. First, on the basis of results obtained by multilocus sequence typing, two very closely related groups were distinguished phylogenetically. However, it appeared that in spite of this phylogenetic proximity, resistance to low pH, bile salts and H2O2 and their capacities of adhesion highly varied from one strain to another. Furthermore, most of the strains reduced the production of the pro-inflammatory interleukin IL-8 after co-incubation with HT-29 cells, while they induced production of the anti-inflammatory interleukin IL-10, when incubated with Peripheral Blood Mononuclear Cells. On the basis of ratio of synthesis of IL-10 and of IL-12, currently used to evaluate the anti-inflammatory potential of a probiotic bacterium, three strains appeared to display a strong and promising in vitro anti-inflammatory potential, suggesting that they could be appropriate for elaborating anti-inflammatory functional fermented foods. Finally, the Principal Component Analysis method enabled us to cluster strains into 6 classes displaying distinct phenotypic properties.
Applied Microbiology and Biotechnology, 100 (8), pp. 3667-3679.
Kebouchi, M., Galia, W., Genay, M., Soligot-Hognon, C., Lecomte, X., Awussi, A. A., Perrin, C., Roux, É., Dary, A., Le Roux, Y.
Streptococcus thermophilus (ST) is a lactic acid
bacterium widely used in dairy industry and displays several
properties which could be beneficial for host. The objective of
this study was to investigate, in vitro, the implication of
sortase A (SrtA) and sortase-dependent proteins (SDPs) in
the adhesion of ST LMD-9 strain to intestinal epithelial cells
(IECs) and resistance to bile salt mixture (BSM;
taurocholoate, deoxycholate, and cholate). The effect of mutations
in prtS (protease), mucBP (MUCin-Binding Protein),
and srtA genes in ST LMD-9 in these mechanisms were examined.
The HT29-MTX, HT29-CL.16E, and Caco-2 TC7
cell lines were used. HT29-MTX and HT29-CL.16E cells
express different mucins found in the gastro intestinal tract;
whereas, Caco-2 TC7 express cell surface proteins found in
the small intestine. All mutants showed different adhesion
profiles depending on cell lines. The mutation in genes srtA
and mucBP leads to a significant decrease in LMD-9 adhesion
capacity to Caco-2 TC7 cells. A mutation in mucBP gene has
also shown a significant decrease inLMD-9 adhesion capacity
to HT29-CL.16E cells. However, no difference was observed
using HT29-MTX cells. Furthermore, ST LMD-9 and srtA
mutant were resistant to BSM up to 3 mM. Contrariwise, no
viable bacteria were detected for prtS and mucBP mutants at
this concentration. Two conclusions could be drawn. First,
SDPs could be involved in the LMD-9 adhesion depending
on the cell lines indicating the importance of eukaryotic-cell
surface components in adherence. Second, SDPs could contribute
to resistance to bile salts probably by maintaining the
cell membrane integrity.
Food Microbiology, 53 (A), pp. 18-29.
Uriot, O., Galia, W., Awussi, A. A., Perrin, C., Denis, S., Chalancon, S., Lorson, É., Poirson, C., Junjua, M., Le Roux, Y., Alric, M., Dary, A., Blanquet-Diot, S., Roussel, Y.
Streptococcus thermophilus, a lactic acid bacterium used to produce yogurts and cheeses is more and more considered for its potential probiotic properties. This implies that additional information should be obtained regarding its survival and metabolic activity in the human Gastro-Intestinal Tract (GIT). In this study, we screened 30 S. thermophilus strains for urease, small heat shock protein, and amino-acid decarboxylase functions which may play a role in survival in the upper part of the GIT. The survival kinetics of 4 strains was investigated using the TIM, a physiologically relevant in vitro dynamic gastric and small intestinal model. The three strains LMD9, PB18O and EBLST20 showed significantly higher survival than CNRZ21 in all digestive compartments of the TIM, which may be related to the presence of urease and heat shock protein functions. When LMD9 bacterial cells were delivered in a fermented milk formula, a significant improvement of survival in the TIM was observed compared to non-fermented milk. With the RIVET (Recombinase In Vivo Expression Technology) method applied to the LMD9 strain, a promoter located upstream of hisS, responsible for the histidyl-transfer RNA synthesis, was found to be specifically activated in the artificial stomach. The data generated on S. thermophilus survival and its adaptation capacities to the digestive tract are essential to establish a list of biomarkers useful for the selection of probiotic strains.
International Dairy Journal, 38 (2), pp. 104-115.
Chang, O.-K., Roux, É., Awussi, A. A., Miclo, L., Jardin, J., Jameh, N., Dary, A., Humbert, G., Perrin, C.
Bioactive peptides can be produced from milk proteins in fermented products by proteases of lactic acid
bacteria. The cell envelope protease (PrtS) of Streptococcus thermophilus is anchored at the cellwall, but we
recently discovered that the 4F44 strain produces a soluble form that can be recovered in medium supernatant.
This workwas aimed at optimising the production of bioactive peptides from bovine caseins. By
growing S. thermophilus 4F44 in the newly designed YLUNi medium, a high quantity of the soluble form of
PrtS could be produced that could be directly used as the proteolytic agent on sodium caseinate. Peptide
production was monitored by reverse phase-high performance liquid chromatography and tandem mass
spectrometry; of 247 peptides identified, 143 were derived from beta-casein. Twenty-two peptides, already
reported in the literature as bioactive, include ACE-inhibitory, antioxidant, immunomodulating, or antibacterial
peptides; addition of such peptides could improve the health benefits of dairy products.
Food Research International, 63 (A), pp. 71-80.
Hafeez, Z., Cakir-Kiefer, C., Roux, É., Perrin, C., Miclo, L., Dary, A.
Besides their basic nutritional role, dietary proteins contain bioactive peptides which are encrypted in their sequence and may modulate different body functions such as digestive, cardiovascular, immune and nervous systems, and therefore contribute in maintaining consumer health. Currently, milk proteins are considered to be the major source of bioactive peptides. The occurrence of these peptides has already been reported in fermented milk products such as yogurt, sour milk or kefir and some of them have been shown to confer health benefits. This review focuses on different strategies that could be employed to enhance the production of bioactive peptides from the milk proteins that will be consequently used to functionalize the fermented milk products. Three types of strategies are developed. The first exploits the proteolytic system of lactic acid bacteria (LAB) or food grade enzymes or combination of both to release the functional peptides from the milk proteins directly in the fermented milk products. The second concerns the supplementation of the fermented milk products with the bioactive peptides obtained outside of the product through the hydrolysis of the purified proteins by the same enzyme sources. Finally, the last consists in the production of the bioactive peptides, initially identified from the milk-proteins, by microorganisms using recombinant DNA technology.
Journal of Dairy Science, 96 (9), pp. 5544-5555.
Chang, O.-K., Seol, K.-H., Jeong, S.-G., Oh, M.-H., Park, B.-Y., Perrin, C., Ham, J.-S.
Applied Microbiology and Biotechnology, 97 (22), pp. 9787-9799.
Hafeez, Z., Cakir-Kiefer, C., Girardet, J.-M., Jardin, J., Perrin, C., Dary, A., Miclo, L.
The trend to confer new functional properties to fermented dairy products by supplementation with bioactive peptides is growing in order to encounter the challenge of health-promoting foods. But these functional ingredients have not to be hydrolysed by proteases of bacteria used in the manufacture of these products. One of the two yoghurt bacteria, Streptococcus thermophilus, has long been considered as weakly proteolytic since its only cell wall-associated subtilisin-like protease, called PrtS, is not always present. Nevertheless, a recent study pointed out a possible peptidase activity in certain strains. In this present study, the stability of milk-derived bioactive peptides, e.g. the anxiolytic peptide, αs1-CN-(f91-97), in the presence of two different S. thermophilus strains with PrtS+ or PrtS− phenotype was studied. Both strains appeared to be capable of hydrolysing the αs1-CN-(f91-97) and other bioactive peptides by recurrent removal of N-terminal residues. The hydrolysis was neither due to intracellular peptidases nor to HtrA protease. Results obtained showed that the observed activity originates from the presence at the surface of both strains of an extracellular aminopeptidase activity. Moreover, a cell wall-associated X-prolyl dipeptidyl peptidase activity was also highlighted when β-casomorphin-7 was used as substrate. All of these findings suggest that, in order to use fermented milks as vector of bioactive peptides, the stability of these bioactive peptides in this kind of products implies to carefully characterize the potential action of the surface proteolytic enzymes of S. thermophilus.
International Dairy Journal, 23 (2), pp. 91-98.
Chang, O.K., Perrin, C., Galia, W., Saulnier, F., Miclo, L., Roux, E., Driou, A., Humbert, G., Dary, A.
PrtS is the sole cell envelope protease (CEP) characterized in Streptococcus thermophilus. It is believed that it is anchored to the cell wall by sortase A (SrtA) through the LPXTG motif present at its C-terminus. Two soluble proteases corresponding to PrtS in its proenzyme and mature form were detected in the supernatant of S. thermophilus strain 4F44. In this strain, 60% of the PrtS molecules are anchored to the cell wall and 40% released in the medium. Such a release might result from a partial deficiency in the strain 4F44 of SrtA, even if its sequence slightly differs from that of S. thermophilus strain LMD-9, in which PrtS is anchored. Indeed, the presence of an intact LPXTG motif at the C-terminus of the released proteases showed that the linking process driven by SrtA did not occur and these proteases were not released by proteolysis after their anchoring.
Journal of Agricultural and Food Chemistry, 60 (2), pp 554-565.
Miclo, L., Roux, E., Genay, M., Brusseaux, E., Poirson, C., Jameh, N., Perrin, C., Dary, A.
Milk proteins contain numerous potential bioactive peptides, which may be released by digestive proteases or by the proteolytic system of lactic acid bacteria during food processing. The capacity of Streptococcus thermophilus to generate peptides, especially bioactive peptides, from bovine caseins was investigated. Strains expressing various levels of the Cell Envelope Proteinase, PrtS, were incubated either with αs1-, αs2- or β-casein. Analysis of the supernatants by LC-ESI-MS/MS showed that the β-casein was preferentially hydrolyzed first, followed by αs2-casein and then αs1-casein. Numbers and types of peptides released were strain-dependent. Hydrolysis appeared to be linked with the accessibility of different casein regions by protease. Analysis of bonds hydrolyzed in the region 1-23 of αs1-casein suggests that PrtS is at least in part responsible for the peptide production. Finally, among the generated peptides, 13 peptides from β-casein, 5 from αs2-casein and 2 from αs1-casein have been reported as bioactive, 15 of them being angiotensin-converting enzyme inhibitors.
Variability and molecular typing of Streptococcus thermophilus strains displaying different proteolytic and acidifying properties
International Dairy Journal, 19 (2), pp. 89-95.
Galia, W., Perrin, C., Genay, M., Dary, A.
Proteolytic and acidifying properties of Streptococcus thermophilus strains isolated from yoghurt or cheeses were evaluated. Among 30 strains tested, 12 exhibited cell envelope-associated proteinase activity (PrtS+), three displayed a slight PrtS activity (PrtS+/−) and 15 were PrtS−, despite the presence of the corresponding gene (prtS) in eight of them. Sequencing of the prtS gene in four PrtS− and one PrtS+ strains revealed that the absence of PrtS activity in the PrtS− strain probably results from an alteration of the prtS regulation. The strains displaying the highest acidifying capacities were all PrtS+. All but one PrtS+ strains were phylogenetically close, as shown by the sequencing of their rDNA internal transcribed spacer (ITS) 16S-23S. More specifically, the high proteolytic and acidifying capacities are associated with the presence of a type II-ITS.
Molecular typing of industrial strains of Pseudomonas spp. isolated from milk and genetical and biochemical characterization of an extracellular protease produced by one of them
International Journal of Food Microbiology, 125 (2), pp. 188-196.
Dufour, D., Nicodème, M., Perrin, C., Driou, A., Brusseaux, E., Humbert, G., Gaillard, J.-L., Dary, A.
Current Microbiology, 48 (1), pp. 51-56.
Nicodème, M., Perrin, C., Hols, P., Bracquart, P., Gaillard, J.-L.
Electrophoresis, 21 (1), pp. 949-955.
Perrin, C., Gonzalez-Marquez, H., Gaillard, J.-L., Bracquart, P., Guimont, C.
Current Microbiology, 39 (1), pp. 342-347.
Perrin, C., Guimont, C., Bracquart, P., Gaillard, J.-L.
Microbiology SGM, 143 (1), pp. 1587-1594.
Gonzalez-Marquez, H., Perrin, C., Bracquart, P., Guimont, C., Linden, G.
22nd International Conference of Functional Food Center (FFC) - 10th International Symposium of Academic Society for Functional Foods and Bioactive Compounds (ASFFBC) at Harvard Medical School, 22-23 septembre, Boston, États-Unis
Hafeez, Z., Perrin, C., Dary, A., Chevalot, I., Kapel, R., Chatel, J.M., Miclo, L.
Inflammation, a basic host defensive response, is crucial for resistance to injury, infectious agents or other noxious stimuli. Nevertheless, excessive and persistent inflammation often leads to various chronic diseases such as cardiovascular, osteoporosis, diabetes, obesity and gastro-intestinal inflammatory diseases. According to WHO, chronic diseases are the leading cause of morbidity and mortality both in developed and developing countries, and represent 60% of all deaths in the world. This figure rises to 87% in Europe and it is expected that more people will be affected by chronic diseases over the next few decades. Increased treatment-related health care costs have made chronic diseases a real health problem to the societies and the concern to prevent or treat these illnesses through diet has increased.
Daily diet is comprised of variety of nutrients including proteins. Bioactive peptides derived from dietary proteins particularly milk may modulate different body functions both at intestinal and systemic levels and ultimately contribute in maintaining consumer health. It has been shown that casein hydrolysates or peptides present in them exhibit anti-inflammatory activity by inhibiting and/or reducing the expression of inflammatory markers and/or by modulating their activity. For example, besides the fragment 106-169 of the bovine κ-casein, anti-inflammatory activity was demonstrated for 84VPP86 and 74IPP76 peptides from the bovine β-casein which reduce in vivo the mRNA expression of inflammatory cytokines (IL-6 and IL-1β). Three ways for releasing peptides from native proteins can be: (i) in vitro enzymatic hydrolysis, (ii) during gastrointestinal digestion or (iii) during fermentation by lactic acid bacteria.
Streptococcus thermophilus, a lactic acid bacterium previously known for conferring organoleptic properties to dairy products, has also been shown to generate bioactive peptides from milk proteins through its cell envelope proteinase (PrtS), which is anchored to cell wall by the transpeptidase sortase SrtA. However, during fermentation the pH decreases due to production of lactic acid and consequently the activity of PrtS is reduced or inhibited (optimal activity at pH 7.5), resulting in lower peptide contents. Therefore, to overcome this problem, S. thermophilus LMD-9-delta-srtA mutant strain was constructed to release in growth medium PrtS, which after purification was used to hydrolyze a caseinate to produce a hydrolysate with higher peptide content, which was afterward fractionated.
The main goal of the study was to evaluate the immunomodulatory potential of the peptide fractions obtained after fractionation by ultrafiltration and diafiltration of a hydrolysate resulting from the hydrolysis of a caseinate by PrtS purified from the growth culture of S. thermophilus LMD-9-delta-srtA strain, using peripheral blood mononuclear cells (PBMC) from 4 human donors.
Materials and Methods:
S. thermophilus LMD-9-delta-srtA strain was cultured for 8 h in yeast-lactose (YL) medium to obtain PrtS-rich supernatant. Followed by batch chromatography using diethylaminoethyl (DEAE) cellulose DE23 (Pharmacia, Uppsala, Sweden) resin and discontinuous gradient of NaCl, PrtS-rich fraction was concentrated by ultrafiltration using Amicon® Ultrafiltration system (cutoff threshold 50 kDa, Milipore, Jaffery, USA). The concentrated PrtS-rich fraction was then used to hydrolyze an industrial caseinate comprising of 87% proteins (92% casein and 8% whey proteins). This initial hydrolyzate (F1) was further fractionated by ultrafiltration using a 3 kDa cut-off membrane to isolate non-hydrolysed proteins in the form of retentate (F2) and peptide fraction as permeate (F3). The F3 fraction was then concentrated by ultrafiltration and diafiltration using a 1 kDa cutoff membrane to obtain retentate (F4) and permeate (F5). The peptide fractions were co-incubated in vitro with PBMCs (Clinisciences, Nanterre, France) and secretion of the IL-10 anti-inflammatory cytokine and of the IL-12 pro-inflammatory cytokine was measured in the cellular medium. The IL-10/IL-12 ratio makes it possible to evaluate the immunomodulatory potential of the peptide fractions.
Using DEAE cellulose DE23 batch chromatography with NaCl gradient, the PrtS was predominantly recovered in the fraction eluted by 0.4 M NaCl since about 90% of the initial activity was found in this fraction. Hydrolysis of caseinate by PrtS was not total since size-exclusion chromatography showed that a significant proportion of proteins remained unhydrolyzed under the conditions used. The protein concentration of the hydrolyzate was about 5 g/L with about 1.6 g/L of peptides. F4 fraction containing peptides whose molecular mass was between 1000 and 3000 Da was free of any salts contrary to F3 and F5 fractions. Anti-inflammatory activity of the five peptide fractions was evaluated by quantifying IL-10 and IL-12 production in vitro after co-incubating individually with PBMCs obtained from four healthy donors who did not use anti-inflammatory drugs for a significant period of time. All the fractions tested at concentrations of 0.2 and 1.0 mg of protein matter / mL led to a secretion of IL-10 by PBMCs except F3 and F5 where the secretion of IL-10 was observed only for concentration of 0.2 mg/mL. The absence of secretion with these fractions tested at 1.0 mg/mL was probably due to an excess of salt content. However, F4 fraction induced higher level of IL-10 production (between 70 and 400 pg/mL according to the PBMC donor) followed by F2 fraction regardless of concentration used. No IL-10 was detected when PBS alone was applied. Similarly, none of the peptide fraction favored the release of the pro-inflammatory cytokine IL-12. Results obtained with the cells of all the donors gave the same conclusions.
PBMC treated with F4 fraction, among all peptide fractions, secreted higher levels of IL-10 in vitro and, therefore, this fraction displayed potential anti-inflammatory activity, as it did not trigger any secretion of IL-12. This peptide fraction is rich in peptides with molecular mass ranging between 1 and 3 kDa. Hence, milk proteins represent a promising source of peptides with potential anti-inflammatory activity and these peptides could be released directly by S. thermophilus or by its protease used as a biotechnological tool. It could be interesting to identify the peptide sequences of the F4 fraction in order to characterize it with the aim of using it in the development of functional fermented milk products.
1er Congrès International de Technologies Alimentaires et Contrôle Qualité des Aliments, 25-27 avril, Djerba, Tunisie
Nasri, W., Jrad, Z., Roux, É., Perrin, C., Girardet, J.-M., Arroum, S., Khorchani, T., El Hatmi, H.
8th NIZO dairy conference, 11-13 Septembre, Papendal, Pays-Bas.
Roux, É., Miclo, L., Chang, O.-K., Humbert, G., Dary, A., Perrin, C.
19e Colloque du Club des Bactéries Lactiques, 16-18 Octobre, Bordeaux, France.
Awussi, A. A., Roux, É., Chang, O.-K., Humbert, G., Dary, A., Perrin, C.
18e Colloque du Club des Bactéries Lactiques, 22-24 mai, Clermont-Ferrand, France
Chang, O.-K., Perrin, C., Roux, É., Miclo, L., Humbert, G., Dary, A.
17e Colloque du Club des Bactéries Lactiques (CBL), 27-29 octobre, Nancy, France
Dary, A., Miclo, L., Cakir-Kiefer, C., Roux, E., Humbert, G., Driou, A., Perrin, C.
17e Colloque du Club des Bactéries Lactiques (CBL), 27-29 octobre, Nancy, France
Hafeez, Z., Cakir-Kiefer, C., Perrin, C., Dary, A., Miclo, L.
17e Colloque du Club des Bactéries Lactiques (CBL), 27-29 octobre, Nancy, France
Jameh, N., Perrin, C., Carré, J., Galia, W., Roux, E., Dary, A.
17e Colloque du Club des Bactéries Lactiques (CBL), 27-29 octobre, Nancy, France
Roux, E., Miclo, L., Brusseaux, E., Poirson, C., Perrin, C., Dary, A.
Actes du séminaire de l'école doctorale RP2E, 28 janvier, Nancy, France.
Jameh, N., Perrin, C., Genay, M., Galia, W., Dary, A.
16e Colloque du Club des Bactéries Lactiques, 27-29 mai, Toulouse, France
Chang O.K., Perrin C., Saulnier F., Driou A., Galia W., Humbert G., Miclo L., Dary A.
Titre : Existence d'une forme extracellulaire de PrtS chez Streptococcus
Auteur(s) : O. K. Chang, C. Perrin, F. Saulnier, A. Driou, W. Galia, G.
L. Miclo et A. Dary
16e Colloque du Club des Bactéries Lactiques, 27-29 mai 2009, Toulouse, France.
4th IDF Dairy Science and Technology Week, 20-24 avril, Rennes, France
Galia, W., Perrin, C., Jameh, N., Genay, M., Dary, A.
Actes du séminaire de l'école doctorale RP2E, 15 janvier, Nancy, France
Chang, O.K., Perrin, C., Driou, A., Galia, W., Humbert, G., Miclo, L., Dary, A.
Rapport de contrat avec le Centre Interprofessionnel de l’Économie Laitière (CNIEL), 55 p.
Miclo, L., Brusseaux, E., Poirson, C., Perrin, C., Dary, A.