Biochemical properties of fodder additives based on fermented poultry wastes and their effects on broiler productivity

V.G. Volik ^a*, D.Yu. Ismailova ^a**, V.S. Lukashenko ^b***, I.P. Saleeva ^b****, T.V. Fedorova ^c*****, E.A. Ovseychik ^b******, E.V. Zhuravchuk ^b*******, S.V. Zinovyev ^a********

^aAll-Russian Research Institute of Poultry Processing Industry, Branch of Federal Scientific Center “All-Russian Research and Technological Poultry Institute”, Russian Academy of Sciences, Rzhavki, 141552 Russia

^bFederal Scientific Center “All-Russian Research and Technological Poultry Institute”, Russian Academy of Sciences, Sergiev Posad, 141311 Russia

^cFederal Research Center “Fundamentals of Biotechnology”, Russian Academy of Sciences, Moscow, 119071 Russia

E-mail: ^*volik@dinfo.ru, ^**dilaramis08@mail.ru, ^***lukashenko@vnitip.ru, ^****saleeva@vnitip.ru, ^*****fedorova_tv@mail.ru, ^******ovseychik@vnitip.ru, ^*******evgeniy_20.02@mail.ru, ^********worklab19@mail.ru

Received March 29, 2019

Full text PDF

DOI: 10.26907/2542-064X.2019.3.422-439

For citation: Volik V.G., Ismailova D.Yu., Lukashenko V.S., Saleeva I.P., Fedorova T.V., Ovseychik E.A., Zhuravchuk E.V., Zinovyev S.V. Biochemical properties of fodder additives based on fermented poultry wastes and their effects on broiler productivity. Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki, 2019, vol. 161, no. 3, pp. 422–439. doi: 10.26907/2542-064X.2019.3.422-439. (In Russian)

Abstract

The wastes of broiler slaughter and carcass processing – poultry by-products (feathers, blood, bones, meat trimmings, etc.) – are the substantial part of the initial live bodyweight of slaughtered broilers (up to 30%); these by-products, with hydrolysates being especially promising, can serve as a source of animal protein in diets for poultry.

In this study, we determined the biochemical properties of the fermented protein additives produced by short-term thermal treatment and subsequent enzymatic hydrolysis of collagen- and keratin-containing poultry wastes.

The dry protein additive based on the keratin-containing wastes featured average moisture content 4.57%, crude protein content 86.52%, crude fat content 2.25%, ash content 2.04%; the respective parameters in the dry additive based on the collagen-containing wastes after high-temperature treatment and enzymatic hydrolysis were 2.57, 45.4, 23.29, and 24.04%.

The digestibility of the dry keratin- and collagen-based additives after the two-stage productive cycle was 92.0 and 85.0%, respectively.

Certain biochemical parameters of these two additives were determined (antioxidative capacity, molecular weight distribution of peptides, profile of volatiles). The analysis of volatiles profile in the keratin-based additive showed that it contained 37 main ingredients, including aliphatic acids and their amides, indole and its derivatives, alcohols, amides of aromatic acids and their derivatives, sulphur-containing substances. The latter are probably responsible for the characteristic odor of the keratin-based product.

It was found that the fermented keratin- and collagen-based additives contain primarily peptides with low (< 5 KDa) and medium (10–25 KDa) molecular weights. The antioxidative capacity of the additives in relation to peroxide radical varied in the range of 250–300 μmoles of trolox equivalent per 1 g; over 99.9% of this capacity was presented by hydrophilic antioxidants.

Trials on broilers with the substitution of the fermented additives for fish meal in the diets proved that the additives do not compromise the growth efficiency and productive performance.

Keywords: fodder additives, keratin-containing poultry wastes, collagen-containing poultry wastes, enzymatic hydrolysis, digestibility, antioxidative capacity, molecular weight distribution, volatile aromatic compounds

Acknowledgments. The study was supported by the Russian Science Foundation (project no. 17-16-01028).

References

1. Kochish I.I., Petrash M.G., Smirnov S.B. Ptitsevodstvo [Poultry Farming]. Moscow, KolosS, 2004. 407 p. (In Russian)
2. Kun K. Ideal ratio of amino acids in the diet of broilers. Kombikorma, 2011, no. 4, pp. 65–70. (In Russian)
3. Fisinin V.I., Imangulov Sh.A. Normirovanie kormleniya sel'skokhozyaistvennoi ptitsy po dostupnym aminokislotam [Balancing Available Amino Acids in Diets for Poultry]. Sergiev Posad, VNITIP, 2000. 47 p. (In Russian)
4. Okolelova T.M., Prosviryakova O.A., Grigor'eva E.N., Shevyakov A.N. A qualitative substitute of fish meal in compound feeds for broilers. Ptitsa Ptitseprod., 2008, no. 2, pp. 41–43. (In Russian)
5. Gonotskii V.A., Fedina L.P., Khvylya S.I., Krasyukov S.N., Abaldova V.A. Myaso ptitsy mekhanicheskoi obvalki [Mechanical Deboning of Poultry Meat]. Moscow, Al'fa-Dizain, 2004. 200 p. (In Russian)
6. Antipova L.V., Sivolotskaya E.V., Polyanskikh S.V. Biotransformation of low-value fluff and feathers into the preparations of amino acids with different degree of purity. Khranenie Pererab. Syr'ya, 2008, no. 1, pp. 59–61. (In Russian)
7. Volik B.G., Ismailova D.Yu., Erokhina O.N., Zinov'ev S.V., Kozak S.S., Mukhin J.E., Koroleva O.V. Efficient use of secondary raw materials obtained in the processing of poultry. Ptitsa Ptitseprod., 2011, no. 3, pp. 16–19. (In Russian)
8. Brenner V.V., Volik V.G., Ismailova D.Yu., Petrovichev V.A., Popov V.O., Chernousov V.I. Method for production of highly digestible protein feed additive for animals and poultry based on short-period thermal treatment of poultry fluff and feathers. Patent RF no. 2018113149, 2019. (In Russian)
9. Volik V.G., Mazur V.M., Ismailova D.Yu., Zinovyev S.V., Gushchin V.V., Erokhina O.N. Method of production of meat-and-bone paste from the wastes of animal and poultry slaughter and processing. Patent RF, no. 2015124144/13, 2016. (In Russian)
10. Maksakov V.Y. Ispol'zovanie vkusovykh i aromaticheskikh veshchestv v kormlenii zhivotnykh [Using Flavoring and Aromatic Substances in Animal Nutrition]. Moscow, Kolos, 1983. 174 p. (In Russian)
11. Sae-Leaw T., O'Callaghan Y.C., Benjakul S., O'Brien N.M. Antioxidant activities and selected characteristics of gelatin hydrolysates from seabass (Lates calcarifer) skin as affected by production processes. J. Food Sci. Technol., 2016, vol. 53, no. 1, pp. 197–208. doi: 10.1007/s13197-015-1989-7.
12. Zhao Q., Shen Q., Guo R., Wu J., Dai Z.-Y. Characterization of flavor properties from fish (Collichthys niveatus) through enzymatic hydrolysis and the Maillard reaction. J. Aquat. Food Prod. Technol., 2016, vol. 25, no. 4, pp. 482–495. doi: 10.1080/10498850.2013.873965.
13. Ross C.F., Smith D.M. Use of volatiles as indicators of lipid oxidation in muscle foods. Compr. Rev. Food Sci. Food Saf., 2006, vol. 5, no. 1, pp.18–25. doi: 10.1111/j.1541-4337.2006.tb00077.x.
14. Varlet V., Knockaert C., Prost C., Serot T. Comparison of odor-active volatile compounds of fresh and smoked salmon. J. Agric. Food Chem., 2006, vol. 54, no. 9, pp. 3391–3401. doi: 10.1021/jf053001p.
15. Nikolaev I.V., Sforza S., Lambertini F., Ismailova D.Yu., Khotchenkov V.P., Volik V.G., Dossena A., Popov V.O., Koroleva O.V. Biocatalytic conversion of poultry processing leftovers: Optimization of hydrolytic conditions and peptide hydrolysate characterization. Food Chem., 2016, vol. 197, pt. A, pp. 611–621. doi: 10.1016/j.foodchem.2015.10.114.
16. Thiansilakul Y., Benjakul S., Richards M.P. Effect of myoglobin from Eastern little tuna muscle on lipid oxidation of washed Asian seabass mince at different pH conditions. J. Food Sci., 2011, vol. 76, no. 2, pp. 242–249. doi: 10.1111/j.1750-3841.2010.01992.x.
17. Kim J.E., Clark R.M., Park Y., Lee J., Fernandez M.L. Lutein decreases oxidative stress and inflammation in liver and eyes of guinea pigs fed a hypercholesterolemic diet. Nutr. Res. Pract., 2012, vol. 6, no. 2, pp. 113–119. doi: 10.4162/nrp.2012.6.2.113.
18. Faustman C., Cassens R. The biochemical basis for discoloration in fresh meat: A review. J. Muscle Foods, 1990, vol. 1, no. 3, pp. 217–243. doi: 10. Ill 1/j. 1745-4573.1990.tb00366.x.
19. Faustman С., Sun Q., Маnсini R., Suman S.P. Myoglobin and lipid oxidation interactions: Mechanistic bases and control. Meat Sci., 2010, vol. 86, no. 1, pp. 86–94. doi: 10.1016/j.meatsci.2010.04.025.
20. Mamelona J., Saint-Louis R., Pelletier E. Nutritional composition and antioxidant properties of protein hydrolysates prepared from echinoderm by-products. Int. J. Food Sci. Technol., 2010, vol. 45, no. 1, pp. 147–154. doi: 10.1111/j.1365-2621.2009.02114.x.
21. Altınelataman C., Koroleva O., Fedorova T., Torkova A., Lisitskaya K., Tsentalovich M., Kononikhin A., Popov I., Vasina D., Kovalyov L., Çelik U. An in vitro and in silico study on the antioxidant and cell culture-based study on the chemoprotective activities of fish muscle protein hydrolysates obtained from European seabass and gilthead seabream. Food Chem., 2019, vol. 271, pp. 724–732. doi: 10.1016/j.foodchem.2018.08.004.
22. Torkova A.A., Ryazantseva K.A., Agarkova E.Yu., Kruchinin A.G., Tsentalovich M.Yu., Fedorova T.V. Rational design of enzyme compositions for the production of functional hydrolysates of cow milk whey proteins. Appl. Biochem. Microbiol., 2017, vol. 53, no. 6. pp. 669–679. doi: 10.1134/S0003683817060138.
23. Kittiphattanabawon P., Benjakul S., Visessanguan W., Shahidi F. Gelatin hydrolysate from blacktip shark skin prepared using papaya latex enzyme: Antioxidant activity and its potential in model systems. Food Chem., 2012, vol. 135, no. 3, pp. 1118–1126. doi: 10.1016/j.foodchem.2012.05.080.

The content is available under the license Creative Commons Attribution 4.0 License.