In the European Union (EU), about five tons of poultry by-product tissues are produced every year. Due to their high collagen content, they represent a significant raw material source for gelatine production. The aim of the paper was the biotechnological preparation of gelatine from chicken feet. The influence of selected process factors on the gelatine yield, gel strength, viscosity, and ash of gelatine was observed; a two-level factor design of experiments with three variable process factors (enzyme addition, enzyme treatment time, and gelatine extraction time) was applied. After grinding and separating soluble proteins and fat, the purified raw material was treated in water at pH 7.5 with the addition of endoprotease at 23 °C and after thorough washing with water at 80 °C, gelatine was extracted. By the suitable choice of process conditions, gelatine with high gel strength (220-320 bloom), low ash content (<2.0%) and viscosity of 3.5-7.3 mPa·s can be prepared. The extraction efficiency was 18-38%. The presented technology is innovative mainly by the enzymatic processing of the source raw material, which is economically, technologically, and environmentally beneficial for manufacturers. Chicken gelatines are a suitable alternative to gelatines made from mammals or fish, and can be used in many food, pharmaceutical, and biomedical applications.

Department of Food Technology Faculty of Technology Tomas Bata University in Zlín Vavrečkova 275 760 01 Zlín Czech Republic

Department of Lipids Detergents and Cosmetics Technology Faculty of Technology Tomas Bata University in Zlín Vavrečkova 275 760 01 Zlín Czech Republic

Department of Polymer Engineering Faculty of Technology Tomas Bata University in Zlín Vavrečkova 275 760 01 Zlín Czech Republic

Zobrazit více v PubMed

Schrieber R., Gareis H. Gelatine Handbook—Theory and Industrial Practice. 1st ed. Wiley-VCH; Weinheim, Germany: 2007. pp. 45–117.

Gómez-Guillén M.C., Giménez B., López-Caballero M.E., Montero M.P. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocoll. 2011;25:1813–1827. doi: 10.1016/j.foodhyd.2011.02.007. DOI

Sheela A.K. Gelatin Market—Global Industry Analysis, Size, Share, Growth, Trends and Forecast, 2012–2018. [(accessed on 22 March 2019)]; Available online: http://www.transparencymarketresearch.com/gelatin.html/

Ferraro V., Anton M., Santé-Lhoutellier V. The “sisters” α-helices of collagen, elastin and keratin recovered from animal by-products: Functionality, bioactivity and trends of application. Trends Food Sci. Technol. 2016;51:65–75. doi: 10.1016/j.tifs.2016.03.006. DOI

The National Agricultural Statistics Service (NASS), United States Department of Agriculture Poultry Slaughter 2016 Summary. [(accessed on 22 March 2019)]; Available online: https://www.nass.usda.gov/Publications/Todays_Reports/reports/pslaan17.pdf/

Eurostat Statistics Explained, Meat Production Statistics for EU-28. [(accessed on 22 March 2019)]; Available online: https://ec.europa.eu/eurostat/statistics-explained/index.php/Meat_production_statistics#Poultry_meat/

Jayathilakan K., Sultana K., Radhakrishna K., Bawa A.S. Utilization of by products and waste materials from meat, poultry and fish processing industries: A review. J. Food Sci. Technol. 2012;49:278–293. doi: 10.1007/s13197-011-0290-7. PubMed DOI PMC

Ockerman H.W., Hansen C.I. Animal By-Product Processing and Utilization. 1st ed. CRC Press; London, UK: 2000. pp. 23–83.

Coutand M., Cyr M., Deydier E., Guilet R., Clastres P. Characteristics of industrial and laboratory meat and bone meal ashes and their potential applications. J. Hazard. Mater. 2008;150:522–532. doi: 10.1016/j.jhazmat.2007.04.133. PubMed DOI

Pitk P., Kaparaju P., Vilu R. Methane potential of sterilized solid slaughterhouse wastes. Bioresour. Technol. 2012;116:42–46. doi: 10.1016/j.biortech.2012.04.038. PubMed DOI

Gómez-Guillœn M.C., Montero M.V.P. Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. J. Food Sci. 2001;66:213–216. doi: 10.1111/j.1365-2621.2001.tb11319.x. DOI

Sinthusamran S., Benjakul S., Kishimura H. Characteristics and gel properties of gelatin from skin of seabass (Lates calcarifer) as influenced by extraction conditions. Food Chem. 2014;152:276–284. doi: 10.1016/j.foodchem.2013.11.109. PubMed DOI

Ahmad M., Benjakul S. Characteristics of gelatin from the skin of unicorn leatherjacket (Aluterus monoceros) as influenced by acid pretreatment and extraction time. Food Hydrocoll. 2011;25:381–388. doi: 10.1016/j.foodhyd.2010.07.004. DOI

Norziah M.H., Al-Hassan A., Khairulnizam A.B., Mordi M.N., Norita M. Characterization of fish gelatin from surimi processing wastes: Thermal analysis and effect of transglutaminase on gel properties. Food Hydrocoll. 2009;23:1610–1616. doi: 10.1016/j.foodhyd.2008.12.004. DOI

Nalinanon S., Benjakul S., Visessanguan W., Kishimura H. Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor. Food Hydrocoll. 2008;22:615–622. doi: 10.1016/j.foodhyd.2007.01.012. DOI

Kasankala L.M., Xue Y., Weilong Y., Hong S.D., He Q. Optimization of gelatine extraction from grass carp (Catenopharyngodon idella) fish skin by response surface methodology. Bioresour. Technol. 2007;98:3338–3343. doi: 10.1016/j.biortech.2006.03.019. PubMed DOI

Cheng F.Y., Hsu F.W., Chang H.S., Lin L.C., Sakata R. Effect of different acids on the extraction of pepsin-solubilised collagen containing melanin from silky fowl feet. Food Chem. 2009;113:563–567. doi: 10.1016/j.foodchem.2008.08.043. DOI

Liu D.C., Lin Y.K., Chen M.T. Optimum condition of extracting collagen from chicken feet and its characteristics. Asian-Australas. J. Anim. Sci. 2001;14:1638–1644. doi: 10.5713/ajas.2001.1638. DOI

Chakka A.K., Muhammed A., Sakhare P.Z., Bhaskar N. Poultry processing waste as an alternative source for mammalian gelatin: Extraction and characterization of gelatin from chicken feet using food grade acids. Waste Biomass Valoriz. 2017;8:2583–2593. doi: 10.1007/s12649-016-9756-1. DOI

Almeida P.F., da Silva Lannes S.C. Extraction and physicochemical characterization of gelatin from chicken by-product. J. Food Process Eng. 2013;36:824–833. doi: 10.1111/jfpe.12051. DOI

Sarbon N.M., Nazlin F.B., Howell K. Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin. Food Hydrocoll. 2013;30:143–151. doi: 10.1016/j.foodhyd.2012.05.009. DOI

Xu M., Wei L., Xiao Y., Bi H., Yang H., Du Y. Physicochemical and functional properties of gelatin extracted from Yak skin. Int. J. Biol. Macromol. 2017;95:1246–1253. doi: 10.1016/j.ijbiomac.2016.11.020. PubMed DOI

Antony J. Design of Experiments for Engineers and Scientists. 1st ed. Butterworth-Heinemann; Oxford, UK: 2003. pp. 54–70.

Du L., Khiari Z., Pietrasik Z., Betti M. Physicochemical and functional properties of gelatins extracted from turkey and chicken heads. Poult. Sci. 2013;92:2463–2474. doi: 10.3382/ps.2013-03161. PubMed DOI

Huda N., Seow E.K., Normawati M.N., Nik Aisyah N.M. Preliminary study on physicochemical properties of duck feet collagen. Int. J. Poult. Sci. 2013;12:615–621. doi: 10.3923/ijps.2013.615.621. DOI

Mrázek P., Mokrejš P., Gál R., Krejčí O. Preparation of collagen concentrate from chicken feet. Waste Forum. 2018;4:444–451.

Mokrejš P., Gál R., Janáčová D., Plšková M., Brychtová M. Chicken paws by-products as an alternative source of proteins. Orient. J. Chem. 2017;33:2209–2216. doi: 10.13005/ojc/330508. DOI

Nollet L.M.L., Toldrá F. Handbook of Food Analysis. 3rd ed. CRC Press; Boca Raton, FL, USA: 2015. pp. 357–754.

ISO 1443:1973 . Meat and Meat Products—Determination of Total Fat Content. ISO; Geneva, Switzerland: 1973.

ISO 937:1978 . Meat and Meat Products—Determination of Nitrogen Content. ISO; Geneva, Switzerland: 1978.

ISO 3496:1994 . Meat and Meat Products—Determination of Hydroxyproline Content. ISO; Geneva, Switzerland: 1994.

Vázquez-Ortiz F.A., González-Méndez N.F. Determination of collagen as a quality index in Bologna from Northwestern Mexico. J. Food Compos. Anal. 1996;9:269–276. doi: 10.1006/jfca.1996.0032. DOI

Standard Testing Methods for Edible Gelatin Official Procedure of the Gelatin Manufacturers Institute of America, Inc. [(accessed on 18 March 2019)]; Available online: http://www.gelatin-gmia.com/images/GMIA_Official_Methods_of_Gelatin_Revised_2013.pdf/

Stange K. Angewandte Statistik Teil 2—Mehrdimensionale Probleme. Springer; Heidelberg, Germany: 1971. pp. 469–495.

Widyasari R., Rawdkuen S. Extraction and characterization of gelatin from chicken feet by acid and ultrasound assisted extraction. Food Appl. Biosci. J. 2014;2:83–95.

Almeida P.F., Calarge F.A., Santana J.C.C. Production of a product similar to gelatin from chicken feet collagen. Eng. Agrícola. 2013;33:1289–1300. doi: 10.1590/S0100-69162013000600021. DOI

Lai J.Y., Lin P.K., Hsiue G.H., Cheng H.Y., Huang S.J., Li Y.T. Low Bloom strength gelatin as a carrier for potential use in retinal sheet encapsulation and transplantation. Biomacromolecules. 2009;10:310–319. doi: 10.1021/bm801039n. PubMed DOI

Lai J.Y., Lu P.L., Chen K.H., Tabata Y., Hsiue G.H. Effect of charge and molecular weight on the functionality of gelatin carriers for corneal endothelial cell therapy. Biomacromolecules. 2006;7:1836–1844. doi: 10.1021/bm0601575. PubMed DOI

Chou S.F., Luo L.J., Lai J.Y., Ma D.H.K. On the importance of Bloom number of gelatin to the development of biodegradable in situ gelling copolymers for intracameral drug delivery. Int. J. Pharm. 2016;511:30–43. doi: 10.1016/j.ijpharm.2016.06.129. PubMed DOI

Bigi A., Panzavolta S., Rubini K. Relationship between triple-helix content and mechanical properties of gelatin films. Biomaterials. 2004;25:5675–5680. doi: 10.1016/j.biomaterials.2004.01.033. PubMed DOI

Lai J.Y. The role of Bloom index of gelatin on the interaction with retinal pigment epithelial cells. Int. J. Mol. Sci. 2009;10:3442–3456. doi: 10.3390/ijms10083442. PubMed DOI PMC

Wang C.S., Virgilio N., Wood-Adams P., Heuzey M.C. A mechanism for the synergistic gelation properties of gelatin B and xanthan gum aqueous mixtures. Carbohydr. Polym. 2017;175:484–492. doi: 10.1016/j.carbpol.2017.08.015. PubMed DOI

Characterization of Fibers Prepared by Centrifugal Spinning from Biotechnologically Derived Chicken Gelatin

Characterization of Poultry Gelatins Prepared by a Biotechnological Method for Targeted Changes at the Molecular Level

Preparation of Gelatin from Broiler Chicken Stomach Collagen

The Effect of Application of Chicken Gelatin on Reducing the Weight Loss of Beef Sirloin after Thawing

Cyprinus carpio Skeleton Byproduct as a Source of Collagen for Gelatin Preparation

Cross-Linked Gelatine by Modified Dextran as a Potential Bioink Prepared by a Simple and Non-Toxic Process

Collagen Hydrolysate Prepared from Chicken By-Product as a Functional Polymer in Cosmetic Formulation

Valorization of a By-Product from the Production of Mechanically Deboned Chicken Meat for Preparation of Gelatins

Polymer Biointerfaces