Rousselot NV

Gent, Belgium

Rousselot NV

Gent, Belgium
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Daneault A.,French National Institute for Agricultural Research | Daneault A.,Clermont University | Prawitt J.,Rousselot SAS | Fabien Soule V.,Rousselot BVBA | And 4 more authors.
Critical Reviews in Food Science and Nutrition | Year: 2017

Osteoporosis is a chronic and asymptomatic disease characterized by low bone mass and skeletal microarchitectural deterioration, increased risk of fracture, and associated comorbidities most prevalent in the elderly. Due to an increasingly aging population, osteoporosis has become a major health issue requiring innovative disease management. Proteins are important for bone by providing building blocks and by exerting specific regulatory function. This is why adequate protein intake plays a considerable role in both bone development and bone maintenance. More specifically, since an increase in the overall metabolism of collagen can lead to severe dysfunctions and a more fragile bone matrix and because orally administered collagen can be digested in the gut, cross the intestinal barrier, enter the circulation, and become available for metabolic processes in the target tissues, one may speculate that a collagen-enriched diet provides benefits for the skeleton. Collagen-derived products such as gelatin or hydrolyzed collagen (HC) are well acknowledged for their safety from a nutritional point of view; however, what is their impact on bone biology? In this manuscript, we critically review the evidence from literature for an effect of HC on bone tissues in order to determine whether HC may represent a relevant alternative in the design of future nutritional approaches to manage osteoporosis prevention. © 2017 Taylor & Francis Group, LLC.

Duconseille A.,French National Institute for Agricultural Research | Astruc T.,French National Institute for Agricultural Research | Quintana N.,Rousselot NV | Meersman F.,Rousselot NV | Sante-Lhoutellier V.,French National Institute for Agricultural Research
Food Hydrocolloids | Year: 2015

Gelatin obtained from pig skin constitutes about 50% of world production and is mainly composed of collagen extracted from skin by acidic baths and thermal treatments. The gelatin is used to make various products, notably hard gelatin capsules (HGC) which of varying solubility in water. This issue has been known for many years and has been, and remains, a subject of study and debate. The main reason for low gelatin dissolution rates is its tendency to form cross-links in the denatured collagen chains under specific conditions which stabilize the gel network and prevent dissolution. As it is extracted from animal tissues, gelatin may contain molecules other than collagen (sugars, lipids and other proteins) which may react with collagen chains to form covalent bonds. Although this biopolymer has been the subject of numerous publications, its structure and composition is not well defined. Indeed, there are many differences from an article to another. Consequently, the causes of HGC dissolution are not well identified and controlled. © 2014 Elsevier Ltd.

Guillerminet F.,French National Institute for Agricultural Research | Guillerminet F.,Agro ParisTech | Guillerminet F.,Rousselot SAS | Beaupied H.,University of Orléans | And 7 more authors.
Bone | Year: 2010

Collagen has an important structural function in several organs of the body, especially in bone and cartilage. The aim of this study was to investigate the effect of hydrolyzed collagen on bone metabolism, especially in the perspective of osteoporosis treatment and understanding of its mechanism of action. An in vivo study was carried out in 12-week-old female C3H/HeN mice. These were either ovariectomized (OVX) or sham-operated (SHAM) and fed for 12 weeks with a diet containing 10 or 25 g/kg of hydrolyzed collagen. We measured bone mineral density (BMD) using dual-energy X-ray absorptiometry (DXA). C-terminal telopeptide of type I collagen (CTX), marker of bone resorption, and alkaline phosphatase (ALP), marker of bone formation, were assayed after 4 and 12 weeks. Femur biomechanical properties were studied by a 3-point bending test and bone architecture by microtomography. The BMD for OVX mice fed the diet including 25 g/kg of hydrolyzed collagen was significantly higher as compared to OVX mice. The blood CTX level significantly decreased when mice were fed with either of the diets containing hydrolyzed collagen. Finally, we have shown a significant increase in bone strength correlated to geometrical changes for the OVX mice fed the 25 g/kg hydrolyzed collagen diet. Primary cultures of murine bone cells were established from the tibia and femur marrow of BALB/c mice. The growth and differentiation of osteoclasts and osteoblasts cultured with different concentrations (from 0.2 to 1.0 mg/mL) of bovine, porcine or fish hydrolyzed collagens (2 or 5 kDa) were measured. Hydrolyzed collagens (2 or 5 kDa) in the tissue culture medium did not have any significant effects on cell growth as compared to controls. However, there was a significant and dose-dependent increase in ALP activity, a well-known marker of osteogenesis, and a decrease in octeoclast activity in primary culture of bone cells cultured with hydrolyzed collagens (2 kDa only) as compared to the control. It is concluded that dietary hydrolyzed collagen increases osteoblast activity (as measured in primary tissue culture), which acts on bone remodeling and increases the external diameter of cortical areas of the femurs. © 2009 Elsevier Inc.

Guillerminet F.,Agro ParisTech | Guillerminet F.,Rousselot SAS | Fabien-Soule V.,Rousselot SAS | Even P.C.,Agro ParisTech | And 4 more authors.
Osteoporosis International | Year: 2012

Summary This study evaluates the effect of hydrolyzed collagen (HC) on bone health of ovariectomized mice (OVX) at different ages. Twenty-six weeks after the OVX procedure, HC ingestion was still able to improve significantly bone mineral density (BMD) and some femur biomechanical parameters. Moreover, HC ingestion for 1 month before surgery prevented BMD decrease. Introduction HC can play an important role in preserving BMD before osteoporosis appears. The aim of this study was to evaluate the effect of HC on bone health of ovariectomized mice at different ages. Methods Female C3H mice were either OVX at 3 or 6 months and fed for 6 months (first experiment) or 3 months (second experiment) with diet including 0, 10, or 25 g/kg of HC. In the second experiment, one group received HC 1 month before surgery, and two groups received the supplementation immediately after surgery, one fed ad libitum and the other by gavage. Mice treated with raloxifene were used as a positive control. BMD, femur intrinsic and extrinsic biomechanical properties, and type I collagen C-terminal telopeptide were measured after 12 and 26 weeks. Food intake and spontaneous physical activity were also recorded. Results The OVX procedure increased body weight, while food intake decreased, thus suggesting that resting metabolism was decreased. Ingestion of 25 g/kg of HC for 3 or 6 months reduced bone loss significantly in, respectively, 3and 6-month-old OVX mice. The lowest HC concentration was less efficient. HC ingestion for 3 months is as efficient as raloxifene to protect 3-month-old OVX mice from bone loss. Our results also demonstrated that HC ingestion before surgery prevented the BMD decreases. Conclusion This study confirms that dietary collagen reduces bone loss in OVX mice by increasing the diameter of the cortical areas of femurs and can have a preventive effect. © 2012 International Osteoporosis Foundation and National Osteoporosis Foundation.

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