Characteristics of Collagen Preparations from Leather Wastes by the High Pressure Liquid Chromatography Method

• Autorzy: Gendaszewska Dorota , Lasoń-Rydel Magdalena , Ławińska Katarzyna , Grzesiak Edyta , Pipiak Paulina

Identyfikatory

DOI

10.5604/01.3001.0014.9308

Warianty tytułu

PL

Charakterystyka preparatów kolagenowych pochodzących z odpadów skórzanych metodą wysokosprawnej chromatografii cieczowej

• Języki publikacji: EN

Abstrakty

EN

The raw trimming waste from the leather industry is considered potential hazardous waste as a consequence of the chrome tanned leather process. On the other hand, leather waste contains a large amount of precious protein – collagen, which has many uses. Nowadays, collagen preparations obtained from leather waste are available on the market. This paper presents a procedure for the determination of amino acids in five collagen preparations of animal origin. Recent improvements in HPLC-based methods for analysing amino acids have made it feasible to analyse different sample types accurately. In this study the 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) derivatization procedure was applied. The amino acid analysis indicated the presence of 18 amino acids (Asp, Ser, Glu, His, Gly, Arg, Thr, Ala, Pro, Cys, Tyr, Val, Lys, Met, Ile, Leu, Phe and Hyp) in the collagen samples. Glycine, alanine, proline and hydroxyproline were the most abundant amino acid, whereas the lowest contents corresponded to serine, tyrosine, valine and izoleucine. The analysis proposed can be used with confidence in collagen quality control to guarantee appropriate amino acid content.

PL

Niegarbowane odpady skórzane pochodzące z przemysłu garbarskiego są potencjalnym zagrożeniem dla środowiska naturalnego. Z drugiej jednak strony tego rodzaju odpady zawierają znaczące ilości cennego białka – kolagenu. Białko kolagenowe jest biopolimerem, który z uwagi na swoje właściwości znajduje zastosowanie w przemyśle spożywczym, kosmetycznym oraz w przemyśle biomedycznym. Obecnie na rynku dostępne są preparaty kolagenowe pozyskane z odpadów pochodzenia zwierzęcego. W pracy przedstawiono procedurę oznaczania aminokwasów w wybranych preparatach kolagenowych metodą wysokosprawnej chromatografii cieczowej i metodą spektrofotometryczną. We wszystkich próbkach oznaczono wysokie stężenia glicyny, alaniny, proliny i hydroksyproliny, a niewielkie ilości tyrozyny, seryny, waliny i izoleucyny. Zastosowana metoda chromatograficzna umożliwia szybkie i równoczesne oznaczenie 17 aminokwasów w badanych próbach. Opracowane w ramach pracy metody analityczne mogą być wykorzystane m.in. do szybkiej kontroli składu aminokwasowego kolagenu.

Słowa kluczowe

EN

amino acid analysis; collagen; leather wastes; HPLC; high pressure liquid chromatography

PL

analiza aminokwasów; kolagen; odpady skórzane; HPLC; wysokosprawna chromatografia cieczowa

• Wydawca: Sieć Badawcza Łukasiewicz - Łódzki Instytut Technologiczny
• Czasopismo: Fibres & Textiles in Eastern Europe
• Rocznik: 2021
• Tom: Vol. 29, no. 5 (149)
• Strony: 75--79
• Opis fizyczny: Bilbiogr. 26 poz., rys., tab.

Twórcy

autor

Gendaszewska Dorota

• Łukasiewicz Research Network – Leather Industry Institute, ul. Zgierska 73, 91-463 Łódź, Poland

• https://orcid.org/0000-0002-9909-0880

autor

Lasoń-Rydel Magdalena

• Łukasiewicz Research Network – Leather Industry Institute, ul. Zgierska 73, 91-463 Łódź, Poland

• https://orcid.org/0000-0003-3490-2638

autor

Ławińska Katarzyna

• Łukasiewicz Research Network – Leather Industry Institute, ul. Zgierska 73, 91-463 Łódź, Poland

• https://orcid.org/0000-0002-0064-3159

autor

Grzesiak Edyta

• Łukasiewicz Research Network – Leather Industry Institute, ul. Zgierska 73, 91-463 Łódź, Poland

autor

Pipiak Paulina

• Łukasiewicz Research Network – Leather Industry Institute, ul. Zgierska 73, 91-463 Łódź, Poland

• https://orcid.org/0000-0002-3546-8258

Bibliografia

• 1. Masilamani D, Madhan B, Shanmugam G, Palanivel S, Narayan B. Extraction of Collagen from Raw Trimming Wastes of Tannery: A Waste to Wealth Approach. Journal of Cleaner Production 2016; 113: 338-344.
• 2. Food and Agriculture Organization of the United Nations, World Statistical Compendium for Raw Hides and Skins, Leather And Leather Footwear 1999-2015. http://www.fao.org/3/a-i5599e.pdf.
• 3. Sanz P, Rucandio I, Cabanillas A. Study Of Cr(VI) in Ashes from Fluidized Bed Combustion of Leather Waste: Applicability of Different Speciation Methods. International Journal of Analytical Chemistry 2003; 83(2): 143-156.
• 4. Poulopoulou VG, Katakisand D, Vrachnou E. A Method for the Removal of Chromium from Tanned Leather Wastes. Journal of the Air & Waste Management Association 1998; 48: 846.
• 5. Yang H, Luo WQ, Guo S, Wen L, Hou C, Shu ZB. Food Science and Technology 2013; 38(2): 98.
• 6. Peng Y, Glattauer V, Werkmeister JA, Ramshaw JAM. Evaluation for Collagen Products for Cosmetic Application. International Journal of Cosmetic Science 2004; 26(6): 313.
• 7. Murali R, Anumary A, Ashokkumar M, Thanikaivelan P, Chandrasekaran B. Hybrid Biodegradable Films from Collagenous Wastes and Natural Polymers for Biomedical Applications. Waste Biomass Valor 2011; 2: 323-335.
• 8. Ławińska K, Lasoń-Rydel M, Gendaszewska D, Grzesiak E, Sieczyńska K, Gaidau C, Epure D-G, Obraniak A. Coating of Seeds with Collagen Hydrolysates from Leather Waste. FIBRES & TEXTILES in Eastern Europe 2019; 27, 4(136): 59-64. DOI: 10.5604/01.3001.0013.1819.
• 9. Parenteau-Bareil R, Gauvin R, Berthod F. Collagen-Based Biomaterials for Tissue Engineering Applications. Materials 2010; 3: 1863-1887.
• 10. Krasnowska G. Characteristics and Use of Collagen Proteins. Veterinary Medicine (in Polish) 2005; 61 (3): 271-274.
• 11. Lapiere CM, Nusgens B, Pierard GE. Interaction Between Collagen Type I and Type III in Conditioning Bundles Organization. Connective Tissue Research 1977; 5(1): 21-29.
• 12. Dimova EY, Nedkov PP, Haertléand T, Nedkov PT. Molecular Mass Disribution and Amino Acid Content of a Cosmetic Collagen Preparation. Biotechnology & Biotechnological Equipment 2014; 14(1): 76-80.
• 13. García-Sifuentes CO, Lugo-Sánchez ME, Scheuren-Aceve S, Martínez-Porchas M, Peralta-Martínez V. Amino Acid Profile of Collagen Fractions Extracted from By-Products of Ophistonema Libertate and Scomber Japonicas. CyTA – Journal of Food 2016; 14(2), 296-301.
• 14. Dent CE. A Study of the Behaviour of Some Sixty Amino-Acids and other Ninhydrin-Reacting Substances on Phenol-; Collidine’ Filter-Paper Chromatograms, with Notes as to the Occurrence of Some of them in Biological Fluids. Biochemical Journal 1948; (2): 169-180.
• 15. Husek P. Gas Chromatography of Amino Acids. Journal of Chromatography 1975; 113(2): 139-230.
• 16. Moore S, Stein WH. Photometric Ninhydrin Method for Use in the Chromatography of Amino Acids. Journal of Biological Chemistry 1948; 176(1): 367.
• 17. Kabelová I, Dvořáková M, Čížková H, Dostálek P, Melzoc K. Determination of free Amino Acids in Cheeses From the Czech Market. Czech Journal of Food Sciences 2009; 27(3): 143.
• 18. Cohen SA, Michaud DP. Synthesis of a Fluorescent Derivatizing Reagent, 6-Aminoquinolyl-N-Hydroxysuccinimidyl Carbamate, and Its Application for the Analysis of Hydrolysate Amino Acids via High-Performance Liquid Chromatography. Analytical Biochemistry 1993; 211: 279-287.
• 19. Reverter M, Lundh T, Lindberg JE. Determination of Free Amino Acids in Pig Plasma by Precolumn Derivatization with 6-N-Aminoquinolyl-N-Hydroxysuccinimidyl Carbamate and High-Performance Liquid Chromatography. Journal of Chromatography B 696 (1): 1-8.
• 20. Woessner JF. The Determination of Hydroxyproline in Tissue and Protein Samples Containing Small Proportions of this Imino Acid. Archives of Biochemistry and Biophysics 1961; 93: 440-447.
• 21. Waters Millipore Corporation, Waters AccQ.Tag Chemistry Package, Instruction manual, USA, 1993.
• 22. BN-85 6149-03. Industry Standard. Raw Materials for Cosmetic Products. Soluble Collagen. Requirements and Tests.
• 23. Jaworska M, Stańczyk M, Wilk M, Kłaczkow G, Anuszewska E, Barzał J, Rzepecki P. New Approach for Amino Acid Profiling in Human Plasma by Selective Fluorescence Derivatization. Amino Acids 2012; 43: 1653.
• 24. Marten S, Naguschewski M. VBS0011N, 05(11), 1 (2011).
• 25. Ignat’eva NYu, Danilov NA, Averkiev SV, Obrezkova MV, Lunin VV, Sobol EN. Determination of Hydroxyproline in Tissues and the Evaluation of the Collagen Content of the Tissues. Journal of Analytical Chemistry 2007; 62(1): 51-57.
• 26. Ward AG, Courts A, editors, The Science and Technology of Gelatin, Academic Press, London, New York, 1977.