Mais la polymyxine n'est pas du tout absorbée dans le sang du système gastro-intestinal et n'a d'effet que dans l'intestin et est utile pour le traitement des infections intestinales azithromycine prix Internet en y faisant des achats permettant d’économiser jusqu'à soixante-dix pour cent, tout en étant sûr de la qualité des produits pharmaceutiques.


ICAMS 2012 – 4th International Conference on Advanced Materials and Systems PROTEIC INGREDIENTS FOR COSMETIC PRODUCTS
MADALINA GEORGIANA ALBU1, IOANNIS IOANIDIS1, MIHAELA VIOLETA GHICA2, VIORICA DESELNICU1, CIPRIAN CHELARU1, GHEORGHE COARA1 1 INCDTP - Division: Leather and Footwear Research Institute, Collagen Department, 93 Ion Minulescu Str, 031215, Bucharest, Romania, [email protected] 2 “Carol Davila” University of Medicine and Pharmacy, Faculty of Pharmacy, Physical and Colloidal Chemistry Department, 6 Traian Vuia Str, 020956, Bucharest, Romania, Hydrolyzed collagen is a natural protein which is successfully used for cosmetic formulationpurposes. The aim of this study was to obtain collagen hydrolysate from wet white leather wasteswhich were pre-tanned with organic (oxazolidine and oxazolidine-resorcinol) and mineral(Titanium-aluminium complex) tanning agents. Solutions of 10% collagen hydrolysates named A,B and C were characterized by dry substance, amide nitrogen, ash, primary amino groups, fatty,pH, FT-IR spectroscopy and rheological analyses. The results demonstrated that the collagenhydrolysate characteristics are influenced by the raw materials (wet white leather) and theproperties allow them to be used in manufacture of cosmetic products.
Keywords: wet white, leather wastes, hydrolysates INTRODUCTION
The cosmetic industry is a field destined to grow rapidly owing to its universal appeal for improving the quality of life (Kligman, 2000). According to Secchi (Secchi,2008) the protein materials for cosmetic purposes are available from ancient time butthe first rational use of proteins in cosmetics dates back to the 1950s. In order to useproteins in water-based cosmetics, they need to be converted into a soluble form, whichis easier to manipulate and is more practical for formulating purposes.
Hydrolyzed collagen is a natural protein derived from the collagen found in animal tissue, especially in skins and bones (Trandafir et al., 2007).
Hydrolysates of non-tanned collagen waste can be advantageously used without further modification as hydration substances in cosmetic preparations (Langmaier et al.,2005).
Leather industry produces a large amount of solid waste containing proteins from skin. In this paper we have investigated the possibilities of using these wastes as asource of protein for the cosmetic industry. As raw material we used two types of wetwhite leather: mineral and organic tanned leather and the obtained hydrolysates werecharacterized by dry substance, amide nitrogen, ash, primary amino groups, fatty, pH,FT-IR spectroscopy and rheological analyses.
Collagen Hydrolysate Preparation
Collagen hydrolysates were prepared by acidic hydrolysis of wet white leather wastes at 125°C during 8 hours according to the technology previously described(Trandafir et al., 2007). The wet white leather wastes were pre-tanned previously withoxazolidine, tinanium-aluminium complex and oxazolidine-resorcinol and liquidhydrolysates were obtained, named hydrolysate A, B and C respectively. They were Proteic Ingredients for Cosmetic Products dried by freeze-drying using the lyophilization program previously described (Albu,2011).
Rheological Analysis
The rheological behaviour of the hydrolysates was evaluated using a rotational viscometer Multi-visc Rheometer-Fungilab. For the determination of the dynamicviscosity, the shear rate and the shear stress the LCP low viscosities adaptor was used.
The rheological experiments were performed at 25°C0.5°C.
FT-IR Analysis
The FT-IR for collagen hydrolysates were recorded using a FT-IR 6000 spectrofotometer with ATR reflection system MK II Golden Gate Single (Jasco). Thespectra were scanned in absorption mode at 4 cm-1 resolution.
The collagen hydrolysate obtained as previously described in materials and methods section were based on wet white wastes pre-tanned with oxazolidine (hydrolisate A), Ti-Al complex (hydrolysate B) and oxazolidine-resorcinol (hydrolysate C).
Oxazolidine is a heterocyclic compound obtained by the reaction of aminohydroxy compounds with aldehydes which has the shrinkage temperature of about 85°C. Thecombination of resorcinol and oxazolidine together as tanning agents increase theshrinkage temperature of above 100°C (Chen and Shana, 2010). Moreover, resorcinolhas low toxicity and is cheap, being used in hair dye intermediates and other cosmeticproducts (Nohynek et al., 2010).
The obtained hydrolysates showed the characteristics presented in the Table 1.
Table 1. Basic characteristics of collagen hydrolysates All the obtained hydrolysates contained high amount of collagen. The amide nitrogen in dry substance is between 17.62 and 17.81, the hydrolysate having very closevalue of molecular weight. Although, the free content of fat allows them to be used incosmetics and medicine.
The rheological analyses of the studied hydrolysates were performed to determine their flow behaviour and their viscosity (Ortan et al., 2011; Dinu-Pîrvu et al., 2012) asthe Figure 1 a-c showed.
ICAMS 2012 – 4th International Conference on Advanced Materials and Systems Figure 1. Rheological behaviour of collagen hydrolysates: a) A hydrolysate; b) B The viscosity is approximately constant for a certain type of hydrolysate, the rheogram shear stress as function of shear rate being consequently linear. From the line Proteic Ingredients for Cosmetic Products slope (Figure 1 a-c) the dynamic viscosity was determined, namely: 0.0275 Pa·s(2.75cP) for hydrolysate A, 0.0241 Pa·s (2.41cP) for hydrolysate B, and 0.0318Pa·s(3.18cP) for hydrolysate C respectively. We can remark that the determinationcoefficient R2 has values superior to 0.9960.
The modifications of collagen structure can be appreciated by the following semiquantitative relations from the FT-IR spectra: - AIII/A1450 ratio, correlated with maintaining of integrity of triple helical structure – values higher or equal to unity indicate preservation of conformation (Albu et al., 2009); - AI/AII ratio, correlated with the hydrolysis degree;The values of AIII/A1450 and AI/AII ratios and the Amide A of all studied hydrolysates are presented in the Table 2 and Figure 2 respectively.
Table 2. Spectral characteristics of collagen hydrolysates Figure 2. Amide A of hydrolysates A, B and C determined by FT-IR spectra From the Table 2 and Figure 2 we can conclude that the integrity of triple helix was over about 70% destroyed and highest degree of hydrolysis was for B hydrolysate. Thiscould be explained due to the strongest cross-linking of pre-tanned leather with organictannins. The FT-IR results are in agreement with rheological ones, B hydrolysate havingalso the smallest viscosity, of 2.41cP.
Three types of collagen hydrolysates were obtained by acidic hydrolysis from wet white leather wastes tanned with oxazolidine, titanium-aluminium complex andoxazolidine-resorcinol. All the obtained hydrolysates contained high amount of collagen ICAMS 2012 – 4th International Conference on Advanced Materials and Systems and the amide nitrogen in dry substance is between 17.62 and 17.81, the hydrolysatehaving very close value of molecular weight. The dynamic viscosity was 2.75cP forhydrolysate A, 2.41cP for hydrolysate B, and 3.18cP for hydrolysate C respectively,with a determination coefficient R2 higher than 0.9960. The FT-IR results are inaccordance with rheology behavior, the properties of hydrolysates allowing them to beused in manufacture of cosmetic products.
This work has been financed by the European Fund for Regional Development and the Romanian Government in the framework of Sectoral Operational Programme underthe project INNOVA-LEATHER: «Innovative technologies for leather sector increasingtechnological competitiveness by RDI, quality of life and environmental protection» –contract POS CCE-AXA 2-O 2.1.2 nr. 242/20.09.2010 ID 638 COD SMIS – CSNR12579.
Albu, M.G. (2011), “Collagen Gels and Matrices for Biomedical Applications”, Lambert Academic Publishing, Saarbrücken, 23-24.
Albu, M.G., Ghica, M.V., Giurginca M. et al. (2009), “Spectral characteristics and antioxidant properties of tannic acid immobiliyed in drug delivery systems”, Revista de Chimie, 60, 666-672.
Chen, H., Shana, Z.H. (2010), “Stabilization of collagen by cross-linking with oxazolidine E-resorcinol”, Journal of Biological Macromolecules, 46(5), 535-539.
Dinu-Pîrvu, C., Ghica, M.V., Ivana, S. et al. (2012), “Formulation and physico-chemical characterization of piroxicam-based carbomer-hydrogels”, AMHB, 1(1), 7-16.
Kligman, A.K. (2000), “A dermatologist looks to the future: promises and problems”, Dermatologic Clinics, Langmaier, F., Mokrejs, P., Karnas, R. et al. (2005), “Modification of chrome-tanned leather waste hydrolysate with epichlorhydrin”, Journal of the Society of Leather Technologists and Chemists, 90, 29-34.
Nohynek, G.J., Antignac, E., Re, T. et al. (2010), “Safety assessment of personal care products/cosmetics and their ingredients”, Toxicology and Applied Pharmacology, 243, 239–259.
Ortan, A., Dinu-Pîrvu, C., Ghica, M.V. et. al. (2011), “Rheological study of a liposomal hydrogel based on carbopol”, Romanian Biotechnological Letter, 16 (1 Suppl.), 47-54.
Secchi, G. (2000), “Role of protein in cosmetics”, Clinics in Dermatology, 26, 321–325.
Trandafir, V., Popescu, G., Albu, M.G. et al. (2007), Collagen-based Bioproducts (in Romanian), Ars


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