PROTEIC INGREDIENTS FOR COSMETIC PRODUCTS

Size: px

Start display at page:

Download "PROTEIC INGREDIENTS FOR COSMETIC PRODUCTS"

Bruce Porter
5 years ago
Views:

1 ICAMS th International Conference on Advanced Materials and Systems PROTEIC INGREDIENTS FOR COSMETIC PRODUCTS MADALINA GEORGIANA ALBU, IOANNIS IOANIDIS, MIHAELA VIOLETA GHICA 2, VIORICA DESELNICU, CIPRIAN CHELARU, GHEORGHE COARA INCDTP - Division: Leather and Footwear Research Institute, Collagen Department, 93 Ion Minulescu Str, 0325, Bucharest, Romania, albu_mada@yahoo.com 2 Carol Davila University of Medicine and Pharmacy, Faculty of Pharmacy, Physical and Colloidal Chemistry Department, 6 Traian Vuia Str, , Bucharest, Romania, mihaelaghica@yahoo.com Hydrolyzed collagen is a natural protein which is successfully used for cosmetic formulation purposes. The aim of this study was to obtain collagen hydrolysate from wet white leather wastes which were pre-tanned with organic (oxazolidine and oxazolidine-resorcinol) and mineral (Titanium-aluminium complex) tanning agents. Solutions of 0% 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 collagen hydrolysate characteristics are influenced by the raw materials (wet white leather) and the properties 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 but the first rational use of proteins in cosmetics dates back to the 950s. In order to use proteins in water-based cosmetics, they need to be converted into a soluble form, which is 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 a source of protein for the cosmetic industry. As raw material we used two types of wet white leather: mineral and organic tanned leather and the obtained hydrolysates were characterized by dry substance, amide nitrogen, ash, primary amino groups, fatty, ph, FT-IR spectroscopy and rheological analyses. MATERIALS AND METHODS Collagen Hydrolysate Preparation Collagen hydrolysates were prepared by acidic hydrolysis of wet white leather wastes at 25 C during 8 hours according to the technology previously described (Trandafir et al., 2007). The wet white leather wastes were pre-tanned previously with oxazolidine, tinanium-aluminium complex and oxazolidine-resorcinol and liquid hydrolysates were obtained, named hydrolysate A, B and C respectively. They were

2 Proteic Ingredients for Cosmetic Products dried by freeze-drying using the lyophilization program previously described (Albu, 20). Rheological Analysis The rheological behaviour of the hydrolysates was evaluated using a rotational viscometer Multi-visc Rheometer-Fungilab. For the determination of the dynamic viscosity, 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). The spectra were scanned in absorption mode at 4 cm - resolution. RESULTS AND DISCUSSION 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. The combination of resorcinol and oxazolidine together as tanning agents increase the shrinkage temperature of above 00 C (Chen and Shana, 200). Moreover, resorcinol has low toxicity and is cheap, being used in hair dye intermediates and other cosmetic products (Nohynek et al., 200). The obtained hydrolysates showed the characteristics presented in the Table. Table. Basic characteristics of collagen hydrolysates Characteristics Hydrolysate A Hydrolysate B Hydrolysate C Dry substance, % Amide nitrogen in dry substance, %.67 / / / 7.69 Proteic substance, % 9.39 / / / Primary amino groups in dry 0.05 / / / 0.66 substance, % Fat in dry substance, % free free free ph for 5% solution All the obtained hydrolysates contained high amount of collagen. The amide nitrogen in dry substance is between 7.62 and 7.8, the hydrolysate having very close value of molecular weight. Although, the free content of fat allows them to be used in cosmetics and medicine. The rheological analyses of the studied hydrolysates were performed to determine their flow behaviour and their viscosity (Ortan et al., 20; Dinu-Pîrvu et al., 202) as the Figure a-c showed.

3 ICAMS th International Conference on Advanced Materials and Systems 7 6 y = x R 2 = Shear stress, Pa a) Shear rate, s - 6 y = x R 2 = Shear stress, Pa b) Shear rate, s y = x R 2 = Shear stress, Pa c) Shear rate, s - Figure. Rheological behaviour of collagen hydrolysates: a) A hydrolysate; b) B hydrolysate; c) C hydrolysate 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

4 Proteic Ingredients for Cosmetic Products slope (Figure a-c) the dynamic viscosity was determined, namely: Pa s (2.75cP) for hydrolysate A, Pa s (2.4cP) for hydrolysate B, and 0.038Pa s (3.8cP) for hydrolysate C respectively. We can remark that the determination coefficient R 2 has values superior to The modifications of collagen structure can be appreciated by the following semiquantitative relations from the FT-IR spectra: - A III /A 450 ratio, correlated with maintaining of integrity of triple helical structure values higher or equal to unity indicate preservation of conformation (Albu et al., 2009); - A I /A II ratio, correlated with the hydrolysis degree; The values of A III /A 450 and A I /A II 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 Sample A III / A 450 A I / A II Hydrolysate A Hydrolysate B Hydrolysate C 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. This could be explained due to the strongest cross-linking of pre-tanned leather with organic tannins. The FT-IR results are in agreement with rheological ones, B hydrolysate having also the smallest viscosity, of 2.4cP. CONCLUSIONS Three types of collagen hydrolysates were obtained by acidic hydrolysis from wet white leather wastes tanned with oxazolidine, titanium-aluminium complex and oxazolidine-resorcinol. All the obtained hydrolysates contained high amount of collagen

5 ICAMS th International Conference on Advanced Materials and Systems and the amide nitrogen in dry substance is between 7.62 and 7.8, the hydrolysate having very close value of molecular weight. The dynamic viscosity was 2.75cP for hydrolysate A, 2.4cP for hydrolysate B, and 3.8cP for hydrolysate C respectively, with a determination coefficient R 2 higher than The FT-IR results are in accordance with rheology behavior, the properties of hydrolysates allowing them to be used in manufacture of cosmetic products. Acknowledgements This work has been financed by the European Fund for Regional Development and the Romanian Government in the framework of Sectoral Operational Programme under the project INNOVA-LEATHER: «Innovative technologies for leather sector increasing technological competitiveness by RDI, quality of life and environmental protection» contract POS CCE-AXA 2-O 2..2 nr. 242/ ID 638 COD SMIS CSNR REFERENCES Albu, M.G. (20), Collagen Gels and Matrices for Biomedical Applications, Lambert Academic Publishing, Saarbrücken, 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, Chen, H., Shana, Z.H. (200), Stabilization of collagen by cross-linking with oxazolidine E-resorcinol, Journal of Biological Macromolecules, 46(5), Dinu-Pîrvu, C., Ghica, M.V., Ivana, S. et al. (202), Formulation and physico-chemical characterization of piroxicam-based carbomer-hydrogels, AMHB, (), 7-6. Kligman, A.K. (2000), A dermatologist looks to the future: promises and problems, Dermatologic Clinics, 8(4), 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, Nohynek, G.J., Antignac, E., Re, T. et al. (200), Safety assessment of personal care products/cosmetics and their ingredients, Toxicology and Applied Pharmacology, 243, Ortan, A., Dinu-Pîrvu, C., Ghica, M.V. et. al. (20), Rheological study of a liposomal hydrogel based on carbopol, Romanian Biotechnological Letter, 6 ( Suppl.), Secchi, G. (2000), Role of protein in cosmetics, Clinics in Dermatology, 26, Trandafir, V., Popescu, G., Albu, M.G. et al. (2007), Collagen-based Bioproducts (in Romanian), Ars Docendi, Bucharest, -2.

6 Proteic Ingredients for Cosmetic Products

DESIGN OF SOME TOPICAL DELIVERY SYSTEMS WITH LIDOCAINE BASED ON COLLAGEN FOR WOUND TREATMENT

DESIGN OF SOME TOPICAL DELIVERY SYSTEMS WITH LIDOCAINE BASED ON COLLAGEN FOR WOUND TREATMENT MIHAELA VIOLETA GHICA 1, MADALINA GEORGIANA ALBU 2, LACRAMIOARA POPA 1 1 Physical-Chemistry and Colloids Department,