TY - JOUR
T1 - An exoproteome approach to monitor safety of a cheese-isolated Lactococcus lactis
AU - Genovese, Federica
AU - Coïsson, Jean Daniel
AU - Majumder, Avishek
AU - Pessione, Alessandro
AU - Svensson, Birte
AU - Jacobsen, Susanne
AU - Pessione, Enrica
N1 - Funding Information:
This work was performed with the financial support of FEMS Research Fellowship 2010 and C.I.B. (Consorzio Interuniversitario per le Biotecnologie) to Federica Genovese and of the Danish Strategic Research Council's Program Committee on Health, Food and Welfare (FøSu) to Avishek Majumder and the EPC group. Part of the funding was supplied by the project CIPE 2006 (Regione Piemonte) . Professor Giuseppe Zeppa (DIVAPRA, Università degli studi di Torino) is thanked for kindly providing the miniature cheeses. Anne Blicher, Bjarne Gregers Schmidt, and Birgit Andersen are thanked for technical assistance. The Typhoon scanner was granted by the Danish Research Council for Natural Science and the Danish Center for Advanced Food Studies contributed to the Bruker Ultraflex II mass spectrometer.
PY - 2013/11
Y1 - 2013/11
N2 - The safety of the cheese-isolated and potential starter Lactococcus lactis 11D was explored by means of an extracellular proteomic study. A preliminary analysis showed good caseification/proteolytic behavior of the strain, absence of production of biogenic amines and good survival at acidic pH. The extracellular proteome map was analyzed to investigate the presence of potential virulence factors. Five moonlighting proteins with adhesive properties (ornithine carbamoyltransferase, fructose bisphosphate aldolase, trigger factor, EF-Tu and GroEL) were identified in the exoproteome, as well as the potential plasminogen binding proteins enolase, GAPDH and phosphoglycerate mutase. Adhesive properties are fundamental features for good starters and commensal strains, although some controversial aspects arise from plasminogen binding proteins as we shall discuss. Noticeably, GroEL, chitinase, and triose phosphate isomerase were abundant in the L. lactis 11D exoproteome. These proteins play a role in bacterial aggregation and in bacteria-fungi interactions, therefore their presence may indicate a good competition potential of the strain against other microorganisms in both food and the gastrointestinal habitat. A DIGE comparative exoproteomic analysis was performed on the L. lactis 11D strain grown on glucose and the disaccharide trehalose, examined here due to its common use as lyophilization stabilizer, respectively. The experiment showed that chitinase biosynthesis was enhanced in presence of trehalose. This is to our knowledge the first extracellular proteomic mapping of L. lactis with relevance for bacterial strain-typing in food safety.
AB - The safety of the cheese-isolated and potential starter Lactococcus lactis 11D was explored by means of an extracellular proteomic study. A preliminary analysis showed good caseification/proteolytic behavior of the strain, absence of production of biogenic amines and good survival at acidic pH. The extracellular proteome map was analyzed to investigate the presence of potential virulence factors. Five moonlighting proteins with adhesive properties (ornithine carbamoyltransferase, fructose bisphosphate aldolase, trigger factor, EF-Tu and GroEL) were identified in the exoproteome, as well as the potential plasminogen binding proteins enolase, GAPDH and phosphoglycerate mutase. Adhesive properties are fundamental features for good starters and commensal strains, although some controversial aspects arise from plasminogen binding proteins as we shall discuss. Noticeably, GroEL, chitinase, and triose phosphate isomerase were abundant in the L. lactis 11D exoproteome. These proteins play a role in bacterial aggregation and in bacteria-fungi interactions, therefore their presence may indicate a good competition potential of the strain against other microorganisms in both food and the gastrointestinal habitat. A DIGE comparative exoproteomic analysis was performed on the L. lactis 11D strain grown on glucose and the disaccharide trehalose, examined here due to its common use as lyophilization stabilizer, respectively. The experiment showed that chitinase biosynthesis was enhanced in presence of trehalose. This is to our knowledge the first extracellular proteomic mapping of L. lactis with relevance for bacterial strain-typing in food safety.
KW - Adhesion
KW - Chitinase
KW - DIGE
KW - Exoproteome
KW - Lactococcus lactis
KW - Plasminogen activation
UR - http://www.scopus.com/inward/record.url?scp=84886308010&partnerID=8YFLogxK
U2 - 10.1016/j.foodres.2012.12.017
DO - 10.1016/j.foodres.2012.12.017
M3 - Article
SN - 0963-9969
VL - 54
SP - 1072
EP - 1079
JO - Food Research International
JF - Food Research International
IS - 1
ER -