Chicken skin gelatine as an alternative to pork and beef gelatines

Authors

  • Petr Mrázek Tomas Bata University in Zlí­n, Faculty of technology, Department of Polymer Engineering, Vavrečkova 275, 760 01, Zlí­n, Czech Republic
  • Pavel Mokrejš Tomas Bata University in Zlí­n, Faculty of technology, Department of Polymer Engineering, Vavrečkova 275, 760 01, Zlí­n, Czech Republic
  • Robert Gál Tomas Bata University in Zlí­n, Faculty of technology, Department of Food Technology, Vavrečkova 275, 760 01 Zlí­n, Czech Republic
  • Jana Orsavová Tomas Bata University in Zlí­n, Faculty of Humanities, Language Centre, Štefánikova 5670, 760 01 Zlí­n, Czech Republic

DOI:

https://doi.org/10.5219/1022

Keywords:

chicken skin, collagen, food grade gelatine, functional properties, poultry by-products

Abstract

Poultry meat-processing industry produces considerably large amounts of by-products (such as chicken skins, heads, feathers, viscera, bones and legs) containing significant volumes of proteins, particularly collagen. One of the possibilities of advantageous utilization of these under-used by-products can be their application as a raw material rich in collagen for preparation of gelatine, a partial hydrolysate of collagen. In the present study, chicken skins obtained as a by-product from the chicken-breast processing were purified from non-collagen proteins, pigments and fats. Collagen was treated with proteolytic enzymes and the gelatine extraction was performed in distilled water at temperatures of 40, 50, 60, 70 and 80 °C during the constant extraction time of 60 min. The influence of the technological conditions on gelatine functional properties including viscosity, clarity, water holding and fat binding capacity, emulsifying and foaming properties was explored. Certain functional properties of prepared gelatines were significantly affected by the extraction temperature, while on some other properties the extraction temperature had no significant effect. Viscosity of prepared chicken skin gelatines was in the range from 3 to 5.7 mPa.s, clarity from 1.5 to 2%, water holding capacity from 3.8 to 5.6 mL.g-1, fat binding capacity from 0.9 to 1.3 mL.g-1, emulsion capacity from 35 to 50%, emulsion stability from 73 to 88%, foaming capacity from 18 to 61% and finally foaming stability was from 4 to 39%. Chicken skin gelatines were compared with commercial food grade pork and beef gelatines. Prepared chicken skin gelatines showed better viscosity, fat binding capacity and foaming stability than mammalian gelatines, while water holding capacity, emulsifying stability and foaming capacity were not as good as in beef and pork gelatines. Emulsifying capacity was comparable with commercial gelatines. Therefore, chicken skin gelatine has the potential as an alternative to traditional gelatines from mammalian sources, such as pork or beef bones and skins.

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

References

Ahmad, M., Benjakul, S. 2011. Characteristics of Gelatin from the Skin of Unicorn Leatherjacket (Aluterus monoceros) as Influenced by Acid Pretreatment and Extraction Time. Food Hydrocolloids, vol. 3, no. 3, p. 25-34. https://doi.org/10.1016/j.foodhyd.2010.07.004 DOI: https://doi.org/10.1016/j.foodhyd.2010.07.004

Bazawine, D., He, Q. 2003. Gelatin: The Paramount food additive. Food Reviews International, vol. 19, no. 4, p. 423-435. https://doi.org/10.1081/FRI-120025483 DOI: https://doi.org/10.1081/FRI-120025483

Bhaskaracharya, R. K., Kentish, S., Ashokkumar, M. 2009. Selected Applications of Ultrasonics in Food Processing. Food Engineering Reviews, vol. 1, no. 1, p. 31-49. https://doi.org/10.1007/s12393-009-9003-7 DOI: https://doi.org/10.1007/s12393-009-9003-7

Bichukale, A. D., Koli, J. M., Sonavane, A. E., Vishwasrao, V. V., Pujari, K. H., Shingare, P. E. 2018. Functional Properties of Gelatin Extracted From Poultry Skin and Bone Waste. International Journal of Pure & Applied Bioscience, vol. 6, no. 4, p. 87-101. https://doi.org/10.18782/2320-7051.6768 DOI: https://doi.org/10.18782/2320-7051.6768

Binsi, P. K., Shamasundar, B. A., Dileep, A. O., Badii, F., Howell, N. K. 2009. Rheological and Functional Properties of Gelatin from the Skin of Bigeye Snapper (Priacanthus Hamrur) Fish. Food Hydrocolloids, vol. 23, no. 1, p. 132-145. https://doi.org/10.1016/j.foodhyd.2007.12.004 DOI: https://doi.org/10.1016/j.foodhyd.2007.12.004

Bower, C. K., Avena‐Bustillos, R. J, Olsen, C. W, McHugh, T. H, Bechtel, P. J. 2006. Characterization of Fish‐Skin Gelatin Gels and Films Containing the Antimicrobial Enzyme Lysozyme. Journal of Food Science, vol. 71, no. 5, p. 141-145. https://doi.org/10.1111/j.1750-3841.2006.00031.x DOI: https://doi.org/10.1111/j.1750-3841.2006.00031.x

Chatterjee S., Bohidar, H. B. 2005. Effect of Cationic Size on Gelation Temperature and Properties of Gelatin Hydrogels. International Journal of Biological Macromolecules, vol. 35, no. 1-2, p. 81-88. https://doi.org/10.1016/j.ijbiomac.2005.01.002 DOI: https://doi.org/10.1016/j.ijbiomac.2005.01.002

Damodaran, S. 2005. Protein Stabilization of Emulsions and Foams. Journal of Food Science and technology, vol. 70, no. 3, p. 54-65. https://doi.org/10.1111/j.1365-2621.2005.tb07150.x DOI: https://doi.org/10.1111/j.1365-2621.2005.tb07150.x

Davídek, J., Hrdlička, J., Karvánek, M., Pokorný, J., Seifert, J., Velíšek, J. 1981. Laboratory guide of food analysis. (Laboratorní příručka analýzy potravin). Prague, Czech Republic : SNTL. 718 p. (in Czech)

Dhakal, D., Koomsap, P., Lamichhane, A., Sadiq, M. B., Anal, A. K. 2018. Optimization of Collagen Extraction From Chicken Feet by Papain Hydrolysis and Synthesis of Chicken Feet Collagen Based Biopolymeric Fibres. Food Bioscience, vol. 23, no. 1, p. 23-30. https://doi.org/10.1016/j.fbio.2018.03.003 DOI: https://doi.org/10.1016/j.fbio.2018.03.003

Djagny, K. B., Wang, Z., Xu, S. 2001. Gelatin: a Valuable Protein for Food and Pharmaceutical Industries: Review. Critical Reviews in Food Science and Nutrition, vol. 4, no. 6, p. 481-492. https://doi.org/10.1080/20014091091904 DOI: https://doi.org/10.1080/20014091091904

GMIA. 2012. Gelatin Handbook. Available at: http://www.gelatin-gmia.com/images/GMIA_Gelatin_Manual_2012.pdf

GMIA. 2013. Standard Testing Methods for Edible Gelatin. Available at: http://www.gelatin-gmia.com/images/GMIA_Official_Methods_of_Gelatin_Revised_2013.pdf

Gómez-Guillén, M. C., Giménez, B., López-Caballero, M. E., Montero, M. P. 2011. Functional and Bioactive Properties of Collagen and Gelatin from Alternative Sources: Review. Food Hydrocolloids, vol. 25, no. 8, p. 1813-1827. https://doi.org/10.1016/j.foodhyd.2011.02.007 DOI: https://doi.org/10.1016/j.foodhyd.2011.02.007

George, N., Joseph, J., Zynudheen, A. 2010. Physical, Mechanical, and Barrier Properties of Carp and Mammalian Skin Gelatin Films. Journal of Food Science, vol. 75, no. 9, p. 620-626. https://doi.org/10.1111/j.1750-3841.2010.01851.x DOI: https://doi.org/10.1111/j.1750-3841.2010.01851.x

Haddar, A., Bougatef, A., Balti, R., Souissi, N., Koched, W., Nasri, M. 2011. Physicochemical and Functional Properties of Gelatin from Tuna (Thunnus Thynnus) Head Bones. Journal of Food and Nutrition Research, vol. 50, no. 3, p. 150-159.

ISO 3496: 1994. Meat and meat products -- Determination of hydroxyproline content

Jain, S., Anal, A., K. 2016. Optimization of Extraction of Functional Protein Hydrolysates from Chicken Egg Shell Membrane (Esm) by Ultrasonic Assisted Extraction (Uae) and Enzymatic Hydrolysis. LWT - Food Science and Technology, vol. 69, no. 1, p. 295-302. https://doi.org/10.1016/j.lwt.2016.01.057 DOI: https://doi.org/10.1016/j.lwt.2016.01.057

Kaewruang, P., Benjakul, S., Prodpran, T., Nalinanon, S. 2013. Physicochemical and Functional Properties of Gelatin from the Skin of Unicorn Leatherjacket (Aluterus Monoceros) as Affected by Extraction Conditions. Food Bioscience, vol. 2, no. 1, p. 1-9. https://doi.org/10.1016/j.fbio.2013.03.002 DOI: https://doi.org/10.1016/j.fbio.2013.03.002

Karim, A., Bhat, R. 2008. Gelatin Alternatives for the Food Industry: Recent Developments, Challenges and Prospects. Trends in Food Science & Technology, vol. 12, no. 12, p. 644-656. https://doi.org/10.1016/j.tifs.2008.08.001 DOI: https://doi.org/10.1016/j.tifs.2008.08.001

Kaur, M., Jumel, K., Hardie, K. R., Hardman, A., Meadows, J., Melia, C. D. 2002. Determining the Molar Mass of a Plasma Substitute Succinylated Gelatin by Size Exclusion Chromatography –Multi- Angle Laser Light Scattering, Sedimentation Equilibrium and Conventional Size Exclusion Chromatography. Journal of Chromatography A, vol. 957, no. 2, p. 139-148. https://doi.org/10.1016/S0021-9673(02)00350-3 DOI: https://doi.org/10.1016/S0021-9673(02)00350-3

Kinsella, J. E. 1976. Functional Properties of Proteins in Foods: a Survey. Critical Reviews in Food Science & Nutrition, vol. 8, no. 3, p. 219-280. https://doi.org/10.1080/10408397609527208 DOI: https://doi.org/10.1080/10408397609527208

Kristinsson, H. G., Rasco, B. A. 2000. Biochemical and Functional Properties of Atlantic Salmon (Salmo Salar) Muscle Proteins Hydrolyzed with Various Alkaline Proteases. Journal of Agricultural and Food Chemistry, vol. 48, no. 3, p. 657-666. https://doi.org/10.1021/jf990447v DOI: https://doi.org/10.1021/jf990447v

Li, F., Jia, D., Yao, K. 2009. Amino acid composition and functional properties of collagen polypeptide from Yak (Bos grunniens) bone. LWT-Food Science and Technology, vol. 42, no. 5, p. 945-949. https://doi.org/10.1016/j.lwt.2008.12.005 DOI: https://doi.org/10.1016/j.lwt.2008.12.005

Mad-Ali, S., Benjakul, S., Prodpran, T., Maqsood, S. 2017. Characteristics and Gelling Properties of Gelatin from Goat Skin as Affected by Drying Methods. Journal of Food Science and Technology, vol. 54, no. 6, p. 1646-1654. https://doi.org/10.1007/s13197-017-2597-5 DOI: https://doi.org/10.1007/s13197-017-2597-5

Masuelli, M. A. 2011. Viscometric Study of Pectin. Effect of Temperature on the Hydrodynamic Properties. International Journal of Biological Macromolecules, vol. 48, no. 2, p. 286-291. https://doi.org/10.1016/j.ijbiomac.2010.11.014 DOI: https://doi.org/10.1016/j.ijbiomac.2010.11.014

Masuelli, M. A., Sansone, M. G. 2012. Hydrodynamic Properties of Gelatin. Studies from Intrinsic Viscosity Measurements, In Verbeek, C. J. R (Ed.). Products and Applications of Biopolymers., InTech, p. 85-116. ISBN 978-953-51-0226-7.

Morrison, N. A., Sworn, G., Clark, R. C., Chen, Y. L., Talashek, T. 1999. Gelatine Alternatives in the Food Industry. In Nishinari K. (eds). Physical Chemistry and Industrial Application of Gellan Gum. Heidelberg: Springer Verlag, p. 127-131. ISBN 978-3-540-48349-6. https://doi.org/10.1007/3-540-48349-7_19 DOI: https://doi.org/10.1007/3-540-48349-7_19

Mrázek, P., Mokrejš, P., Gál, R., Orsavová, J. 2019. Assessment of possibilities of food grade gelatines preparation from chicken skin. In Mendelnet Conference, Brno, Czech Republic: Mendelnet University Brno, in press.

Nasrin, T. A. A., Noomhorm, A., Anal, A. K. 2015. Physico-chemical characterization of culled plantain pulp starch, peel starch and flour. International Journal of Food Properties, vol. 18, no. 1, p. 165-177. https://doi.org/10.1080/10942912.2013.828747 DOI: https://doi.org/10.1080/10942912.2013.828747

Neto, V. Q., Narain, N., Silva, J. B., Bora, P. S. 2001. Functional Properties of Raw and Heat Processed Cashew Nut (Anarcardium occidentale L.) Kernel Protein Isolates. Nahrung/Food, vol. 45, no. 4, p. 258-262. https://doi.org/10.1002/1521-3803(20010801)45:4<258::AID-FOOD258>3.0.CO;2-3 DOI: https://doi.org/10.1002/1521-3803(20010801)45:4<258::AID-FOOD258>3.0.CO;2-3

Ninan, G., Joseph, J., Aliyamveettil, Z. 2014. A Comparative Study on the Physical, Chemical and Functional Properties of Carp Skin and Mammalian Gelatins. Journal of Food Science and Technology, vol. 51, no. 9, p. 2085-2091. https://doi.org/10.1007/s13197-012-0681-4 DOI: https://doi.org/10.1007/s13197-012-0681-4

Norziah, M. H, Al-Hassan, A., Khairulnizam, A. B., Mordi, M. N., Norita, M. 2009. Characterization of Fish Gelatin from Surimi Processing Wastes. Food Hydrocolloids, vol. 23, no. 6, p. 1610-1616. https://doi.org/10.1016/j.foodhyd.2008.12.004 DOI: https://doi.org/10.1016/j.foodhyd.2008.12.004

Ockerman, H. W., Hansen, C. L. 2000. Animal By-Product Processing & Utilization. Lancaster: Technomic Pub. Co. 544 p. ISBN 1566767776. DOI: https://doi.org/10.1201/9781482293920

Omar, W., Sarbon, N. 2016. Effect of Drying Method on Functional Properties and Antioxidant Activities of Chicken Skin Gelatin Hydrolysate. Journal of Food Science and Technology, vol. 53, no. 11, p. 3928-3938. https://doi.org/10.1007/s13197-016-2379-5 DOI: https://doi.org/10.1007/s13197-016-2379-5

Petrášová, M., Zichová, E., Pospiech, M., Tremlová, B., Javůrková, Z. 2016. Possibilities of Microscopic Detection of Isolated Porcine Proteins in Model Meat Products. Potravinarstvo, vol. 10, no. 1, p. 202-206. https://doi.org/10.5219/588 DOI: https://doi.org/10.5219/588

Qiao, C., Chen, G., Li, Y., Li, T. 2013. Viscosity Properties of Gelatin in Solutions of Monovalent and Divalent Salts. Korea-Australia Rheology Journal, vol. 25, no. 4, p. 227-231. https://doi.org/10.1007/s13367-013-0023-8 DOI: https://doi.org/10.1007/s13367-013-0023-8

Rafieian, F., Keramat, J., Kadivar, M. 2011. Optimization of Gelatin Extraction from Chicken Deboner Residue Using RSM Method. Journal of food science and technology, vol. 50, no. 2, p. 374-80. https://doi.org/10.1007/s13197-011-0355-7 DOI: https://doi.org/10.1007/s13197-011-0355-7

Raju, A. A., Rose, C., Rao, N. M. 1997. Enzymatic Hydrolysis of Tannery Fleshings Using Chciken intestine Proteases. Animal Feed Science and technology, vol. 66, no.1-4, p. 139-147. https://doi.org/10.1016/S0377-8401(96)01109-1 DOI: https://doi.org/10.1016/S0377-8401(96)01109-1

Rawdkuen, S., Thitipramote, N., Benjakul, S. 2013. Preparation and Functional Characterisation of Fish Skin Gelatin and Comparison with Commercial Gelatin. International Journal of Food Science & Technology, vol. 48, no. 5, p. 1093-1102. https://doi.org/10.1111/ijfs.12067 DOI: https://doi.org/10.1111/ijfs.12067

Salminen, E. A., Rintala, J. 2002. Anaerobic Digestion of Organic Solid Poultry Slaughterhouse Waste – a Review. Bioresource Technology, vol. 83, no. 1, p. 13-26. https://doi.org/10.1016/S0960-8524(01)00199-7 DOI: https://doi.org/10.1016/S0960-8524(01)00199-7

Sathe, S. K., Deshpande, S. S., Salunkhe, D. K. 1982. Functional properties of lupin seed (Supinus mutabilis) proteins and protein concentrates. Journal of Food Science, vol. 7, no. 2, p. 191-197. https://doi.org/10.1111/j.1365-2621.1982.tb10110.x DOI: https://doi.org/10.1111/j.1365-2621.1982.tb10110.x

Shahidi, F., Xiao-Qing, H., Synowiecki, J. 1995. Production and characteristics of protein hydrolysates from Capelin (Mallotus-villosus). Food Chemistry, vol. 53, no. 3, p. 285-293. https://doi.org/10.1016/0308-8146(95)93934-J DOI: https://doi.org/10.1016/0308-8146(95)93934-J

Sheela, A. K. 2014. Gelatin Market by Raw Material (Pig Skin, Bovine Hide, Bones and Others) for Food & Beverage, Nutraceuticals, Pharmaceuticals, Photography, Cosmetics and Other Applications – Global Industry Analysis, Size, Share, Growth, Trends and Forecast, 2012–2018. Available at: http://www.transparencymarketresearch.com/gelatin.html

Sheu, K. S., Chen, T. C. 2002. Yield and Quality Characteristics of Edible broiler Skin Fat as Obtained from Five rendering methods. Journal of Food Engineering, vol. 55, no. 3, p. 263-269. https://doi.org/10.1016/S0260-8774(02)00100-0 DOI: https://doi.org/10.1016/S0260-8774(02)00100-0

Simões, G. S., Silveira, E. T. F., De Oliveira, S. R., Poleze, E., Allison, J. R., Ida, E. I., Shimokomaki, M. 2014. Optimum Conditions for Extracting Collagen from the Tunica Albuginea of Immunologically Castrated Pig Testes and the Functional Properties of the Isolated Collagen. Meat Science, vol. 96, no. 4, p. 1460-1468. https://doi.org/10.1016/j.meatsci.2013.10.038 DOI: https://doi.org/10.1016/j.meatsci.2013.10.038

Souissi, N., Bougatef, A., Triki-Ellouz, Y., Nasri, M. 2007. Biochemical and Functional Properties of Sardinella (Sardinella aurita) By-product Hydrolysates. Food technology and Biotechnology, vol. 45, no. 2, p. 187-194.

Surangna, J., Anal, A. K. 2016. Optimization of Extraction of Functional Protein Hydrolysates from Chciken Egg Shell membrane (ESM) by Ultrasonic Assisted Extraction (UAE) and Enzymatic Hydrolysis. Food Science and technology, vol. 69, no. 1, p. 295-302. https://doi.org/10.1016/j.lwt.2016.01.057 DOI: https://doi.org/10.1016/j.lwt.2016.01.057

Toldra, F., Mora, L., Reig, M. 2016. New Insights into Meat By-Product Utilization. Meat Science, vol. 120, no. 1, p. 54-59. https://doi.org/10.1016/j.meatsci.2016.04.021 DOI: https://doi.org/10.1016/j.meatsci.2016.04.021

Wilding, P., Lilliford, P. J., Regenstein, J. M. 1984. Functional Properties of Proteins in Foods. Journal of Chemical Technology and Biotechnoogy, vol. 34, no. 3, 182 p. https://doi.org/10.1002/jctb.280340307 DOI: https://doi.org/10.1002/jctb.280340307

Zarai, Z., Balti, R., Mejdoub, H., Gargouri, Y., Sayari, A. 2012. Process for Extracting Gelatin from Marine Snail (Hexaplex Trunculus): Chemical Composition and Functional Properties. Process Biochemistry, vol. 47, no. 12, p. 1779-1784. https://doi.org/10.1016/j.procbio.2012.06.007 DOI: https://doi.org/10.1016/j.procbio.2012.06.007

Zhou, P., Mulvaney, S. J., Regenstein, J. M. 2006. Properties of Alaska Pollock Skin Gelatin. Journal of Food Science, vol. 71, no. 6, p. 313-321. https://doi.org/10.1111/j.1750-3841.2006.00065.x DOI: https://doi.org/10.1111/j.1750-3841.2006.00065.x

Zhu, G. Y., Zhu, X., Wan, X. L., Fan, Q., Ma, Y. H., Qian, J., Liu, X. L., Shen., Y. J., Jiang, J. H. 2010. Hydrolysis Technology and Kinetics of Poultry Waste to Produce Amino Acids in Subcritical Water. Journal of Analytical and Applied Pyrolysis, vol. 88, no. 2, p. 187-191. https://doi.org/10.1016/j.jaap.2010.04.005 DOI: https://doi.org/10.1016/j.jaap.2010.04.005

Published

2019-03-23

How to Cite

Mrázek, P. ., Mokrejš, P. ., Gál, R. ., & Orsavová, J. . (2019). Chicken skin gelatine as an alternative to pork and beef gelatines. Potravinarstvo Slovak Journal of Food Sciences, 13(1), 224–233. https://doi.org/10.5219/1022

Most read articles by the same author(s)