Christine DELBARRE-LADRAT

Dr. Christine DELBARRE-LADRAT

Ifremer, Laboratoire Ecosystèmes Microbiens et Molécules Marines pour les Biotechnologies EM3B, 44311 Nantes, France
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Research Focus & Metrics

Academic Career Length

30Years (1997-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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23 September 2011 in Marine Drugs
Verified
Journal Article
Open access
PDF file
SKSenni Karim
Senni Karim
JPJessica Pereira
Jessica Pereira
FGFarida Gueniche
Farida Gueniche
CDChristine DELBARRE-LADRAT
Christine DELBARRE-LADRAT
CSCorinne Sinquin
Corinne Sinquin
Sylvia Colliec-JouaultSylvia Colliec-Jouault
Sylvia Colliec-Jouault
The therapeutic potential of natural bioactive compounds such as polysaccharides, especially glycosaminoglycans, is now well documented, and this activity combined with natural biodiversity will allow the development of a new generation of therapeutics. Advances in our understanding of the biosynthesis, structure and function of complex glycans from mammalian origin have shown the crucial role of this class of molecules to modulate disease processes and the importance of a deeper knowledge of structure-activity relationships. Marine environment offers a tremendous biodiversity and original polysaccharides have been discovered presenting a great chemical diversity that is largely species specific. The study of the biological properties of the polysaccharides from marine eukaryotes and marine prokaryotes revealed that the polysaccharides from the marine environment could provide a valid alternative to traditional polysaccharides such as glycosaminoglycans. Marine polysaccharides present a real potential for natural product drug discovery and for the delivery of new marine derived products for therapeutic applications.

1 June 2006 in Critical Reviews in Food Science and Nutrition
Verified
Journal Article
Closed access
CDChristine DELBARRE-LADRAT
Christine DELBARRE-LADRAT
RCRomuald Chéret
Romuald Chéret
RTRichard Taylor
Richard Taylor
VVVéronique Verrez-Bagnis
Véronique Verrez-Bagnis
Postmortem tenderization is caused by enzymatic degradation of key structural proteins in myofibrils as well as in extracellular matrix, and of proteins involved in intermyofibrillar linkages and linkages between myofibrils and the sarcolemma. The function of these proteins is to maintain the structural integrity of myofibrils. Current data indicate that calpains and cathepsins may be responsible for degradation of these proteins. Other phenomena occurring in cells postmortem (pH drop, sarcoplasmic Ca 2+ increase, osmotic pressure rise, oxidative processes) may act in synergy with proteases. Our understanding of the underlying mechanisms of muscle degradation should be improved for an accurate evaluation of the postmortem muscle changes and consequently of the fish quality.

1 October 2005 in Journal of Food Science
Verified
Journal Article
Closed access
PDF file
RCRomuald Chéret
Romuald Chéret
NCNicolas Chapleau
Nicolas Chapleau
CDChristine DELBARRE-LADRAT
Christine DELBARRE-LADRAT
VVVéronique Verrez-Bagnis
Véronique Verrez-Bagnis
MLMarie de Lamballerie
Marie de Lamballerie

1 January 2007 in Food Chemistry
Verified
Journal Article
Closed access
RCR Cheret
R Cheret
CDChristine DELBARRE-LADRAT
Christine DELBARRE-LADRAT
MLM Lamballerieanton
M Lamballerieanton
VVVéronique Verrez-Bagnis
Véronique Verrez-Bagnis

1 January 2008 in Biofouling
Verified
Journal Article
Closed access
CLC. Leroy
C. Leroy
CDChristine DELBARRE-LADRAT
Christine DELBARRE-LADRAT
FGF. Ghillebaert
F. Ghillebaert
CCC. Compere
C. Compere
DCD. Combes
D. Combes
The antifouling potential of commercial hydrolases, four proteases, seven glycosidases and one lipase was evaluated on the adhesion of marine Pseudoalteromonas sp. D41. The experimental method, adapted to screen antifouling agents, was based on bacterial adhesion in natural sterile sea water in a microtiter plate and on total biomass quantification by the fluorescent dye DAPI (4[prime]6-diamidino-2-phenylindole). Savinase (subtilisin) was the most effective hydrolase in both the prevention of bacterial adhesion and the removal of adhered bacteria. However, some enzymatic preparations tested such as Amano protease were not only ineffective but also increased the number of adhered bacterial cells. Enumeration using epifluorescence microscopy of CTC (5-cyano-2,3-ditolyl tetrazolium chloride) and DAPI stained adhered D41 cells confirmed these observations. Overall, these results demonstrated that hydrolases could either prevent adhesion and remove adhered bacterial cells effectively, or conversely increase bacterial adhesion, depending on enzymatic concentrations and the type of enzymes tested.