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Compound enzymatic hydrolysis of feather waste to improve the nutritional value

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Abstract

Although feather waste is generated abundantly but rich in natural protein, it is hassled to be digested. To improve the nutritional value of feather waste, compound enzymatic hydrolysis (CEH) was applied to degrade feather waste. Results indicated that the nutritional value of feather meal (FM) produced with CEH was improved in terms of protein solubility increase to 20.75 times and in vitro protein digestibility increase to 10.27 times as compared to fresh FM; this improvement was ascribed to the keratinase breaking up disulfide bond and compound enzymes destroying the smooth surface structure, compact β-sheet structure, and hydrogen bond. In conclusion, CEH is an effective and promising approach to improve the nutrient value of feather waste. The results shed light on the utilization of feather waste for protein resource in feed industry.

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References

  1. Sharma S, Gupta A (2016) Sustainable management of keratin waste biomass: applications and future perspectives. Braz Arch Biol Technol 59, e16150684

  2. Mazotto A, Ascheri J, de Oliveira GR (2017) Production of feather protein hydrolyzed by B. subtilis AMR and its application in a blend with cornmeal by extrusion. LWT Food Sci Technol 84:701–709

    Google Scholar 

  3. Campos I, Matos E, Marques A, Valente LM (2017) Hydrolyzed feather meal as a partial fishmeal replacement in diets for European seabass (Dicentrarchus labrax) juveniles. Aquaculture 476:152–159

    Google Scholar 

  4. Tiwary E, Gupta R (2012) Rapid conversion of chicken feather to feather meal using dimeric keratinase from Bacillus licheniformis ER-15. J Bioprocess Biotech 2:2

    Google Scholar 

  5. Zhang Y, Yang R, Zhao W (2014) Improving digestibility of feather meal by steam flash explosion. J Agric Food Chem 62:2745–2751

    Google Scholar 

  6. Lemes AC, Álvares GT, Egea MB, Brandelli A, Kalil SJ (2016) Simultaneous production of proteases and antioxidant compounds from agro-industrial by-products. Bioresour Technol 222:210–216

    Google Scholar 

  7. Poovendran P, Kalaigandhi V, Kanan V, Rani E, Poongunran E (2011) A study of feather keratin degradation by Bacillus licheniformis and quantification of keratinase enzyme produced. J Microbiol Biotechnol Res 1:120–126

  8. Korniłłowicz-Kowalska T, Bohacz J (2011) Biodegradation of keratin waste: theory and practical aspects. Waste Manag 31:1689–1701

    Google Scholar 

  9. Yang L, Wang H, Lv Y, Bai Y, Luo H, Shi P, Huang H, Yao B (2015) Construction of a rapid feather-degrading bacterium by overexpression of a highly efficient alkaline keratinase in its parent strain Bacillus amyloliquefaciens K11. J Agric Food Chem 64:78–84

    Google Scholar 

  10. Bohacz J (2017) Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss. World J Microb Biot 33:13

    Google Scholar 

  11. Gupta R, Ramnani P (2006) Microbial keratinases and their prospective applications: an overview. Appl Microbiol Biotechnol 70:21–33

    Google Scholar 

  12. Vidmar B, Vodovnik M (2018) Microbial keratinases: enzymes with promising biotechnological applications. Food Technol Biotechnol 56:312–328

    Google Scholar 

  13. Bach E, Daroit DJ, Correa AP, Brandelli A (2011) Production and properties of keratinolytic proteases from three novel gram-negative feather-degrading bacteria isolated from Brazilian soils. Biodegradation 22:1191–1201

    Google Scholar 

  14. Yamamura S, Morita Y, Hasan Q, Yokoyama K, Tamiya E (2002) Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp. Biochem Biophys Res Commun 294:1138–1143

    Google Scholar 

  15. Peng Q, Khan NA, Wang Z, Yu P (2014) Relationship of feeds protein structural makeup in common prairie feeds with protein solubility, in situ ruminal degradation and intestinal digestibility. Anim Feed Sci Technol 194:58–70

    Google Scholar 

  16. Yan X, Khan NA, Zhang F, Yang L, Yu P (2014) Microwave irradiation induced changes in protein molecular structures of barley grains: relationship to changes in protein chemical profile, protein subfractions, and digestion in dairy cows. J Agric Food Chem 62:6546–6555

    Google Scholar 

  17. Emmambux MN, Taylor JR (2009) Properties of heat-treated sorghum and maize meal and their prolamin proteins. J Agric Food Chem 57:1045–1050

    Google Scholar 

  18. Xie X, Guo X, Zhou L, Yao Q, Zhu H (2019) Study of biochemical and microbiological properties during co-composting of spent mushroom substrates and chicken feather. Waste Biomass Valorization 10:23–32

    Google Scholar 

  19. Moritz J, Latshaw J (2001) Indicators of nutritional value of hydrolyzed feather meal. Poultry Sci 80:79–86

    Google Scholar 

  20. Eaksuree W, Prachayakitti A, Upathanpreecha T, Taharnklaew R, Nitisinprasert S, Keawsompong S (2016) In vitro and in vivo evaluation of protein quality of enzymatic treated feather meals. SpringerPlus 5:971

    Google Scholar 

  21. Ravindran G, Ravindran V, Bryden WL (2006) Total and ileal digestible tryptophan contents of feedstuffs for broiler chickens. J Sci Food Agric 86:1132–1137

    Google Scholar 

  22. Radha S, Gunasekaran P (2007) Cloning and expression of keratinase gene in Bacillus megateriumand optimization of fermentation conditions for the production of keratinase by recombinant strain. J Appl Microbiol 103:1301–1310

    Google Scholar 

  23. Kim JD (2007) Purification and characterization of a keratinase from a feather-degrading fungus, Aspergillus flavus strain K-03. Mycobiology 35:219–225

    Google Scholar 

  24. Wang T, Johnson LA (2001) Survey of soybean oil and meal qualities produced by different processes. J Am Oil Chem Soc 78:311–318

    Google Scholar 

  25. Wang X, Gao W, Zhang J, Zhang H, Li J, He X, Ma H (2010) Subunit, amino acid composition and in vitro digestibility of protein isolates from Chinese kabuli and desi chickpea (Cicer arietinum L.) cultivars. Food Res Int 43:567–572

    Google Scholar 

  26. Grazziotin A, Pimentel F, De Jong E, Brandelli A (2006) Nutritional improvement of feather protein by treatment with microbial keratinase. Anim Feed Sci Technol 126:135–144

    Google Scholar 

  27. Wang C, Jiang L, Wei D, Li Y, Sui X, Wang Z, Li D (2011) Effect of secondary structure determined by FTIR spectra on surface hydrophobicity of soybean protein isolate. Procedia Eng 15:4819–4827

    Google Scholar 

  28. Stein HH, Lagos L, Casas G (2016) Nutritional value of feed ingredients of plant origin fed to pigs. Anim Feed Sci Technol 218:33–69

    Google Scholar 

  29. Dahl L (1960) Effects of chronic excess salt feeding: elevation of plasma cholesterol in rats and dogs. J Exp Med 112:635–651

    Google Scholar 

  30. Morr C, German B, Kinsella J, Regenstein J, Buren JV, Kilara A, Lewis B, Mangino M (1985) A collaborative study to develop a standardized food protein solubility procedure. J Food Sci 50:1715–1718

    Google Scholar 

  31. Parsons CM, Hashimoto K, Wedekind KJ, Baker DH (1991) Soybean protein solubility in potassium hydroxide: an in vitro test of in vivo protein quality. J Anim Sci 69:2918–2924

    Google Scholar 

  32. Panyam D, Kilara A (1996) Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci Technol 7:120–125

    Google Scholar 

  33. Tao LY, Gong JS, Su C, Jiang M, Li H, Li H, Lu ZM, Xu ZH, Shi JS (2018) Mining and expression of a metagenome-derived keratinase responsible for biosynthesis of silver nanoparticles. ACS Biomater Sci Eng 4:1307–1315

    Google Scholar 

  34. Prakash P, Jayalakshmi SK, Sreeramulu K (2010) Purification and characterization of extreme alkaline, thermostable keratinase, and keratin disulfide reductase produced by Bacillus halodurans PPKS-2. Appl Microbiol Biotechnol 87:625–633

    Google Scholar 

  35. Wubshet SG, Måge I, Böcker U, Lindberg D, Knutsen SH, Rieder A, Rodriguez DA, Afseth NK (2017) FTIR as a rapid tool for monitoring molecular weight distribution during enzymatic protein hydrolysis of food processing by-products. Anal Methods UK 9:4247–4254

    Google Scholar 

  36. Kim EJ, Utterback PL, Parsons CM (2012) Comparison of amino acid digestibility coefficients for soybean meal, canola meal, fish meal, and meat and bone meal among 3 different bioassays. Poult Sci 91:1350–1355

    Google Scholar 

  37. Adler SA, Slizyte R, Honkapaa K, Loes AK (2018) In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers. Poult Sci 97:3343–3357

    Google Scholar 

  38. Łaba W, Chorążyk D, Pudło A, Trojan-Piegza J, Piegza M, Kancelista A, Kurzawa A, Żuk I, Kopeć W (2017) Enzymatic degradation of pretreated pig bristles with crude keratinase of Bacillus cereus PCM 2849. Waste Biomass Valori 8:527–537

    Google Scholar 

  39. Dust JM, Grieshop C, Parsons CM, Karr-Lilienthal L, Schasteen C, Quigley J III, Merchen NR, Fahey G Jr (2005) Chemical composition, protein quality, palatability, and digestibility of alternative protein sources for dogs. J Anim Sci 83:2414–2422

    Google Scholar 

  40. Coward-Kelly G, Chang VS, Agbogbo FK, Holtzapple MT (2006) Lime treatment of keratinous materials for the generation of highly digestible animal feed: 1. Chicken Feathers Bioresour Technol 97:1337–1343

    Google Scholar 

  41. Brito OJ, Nunez N (1982) Evaluation of sesame flour as a complementary protein source for combinations with soy and corn flours. J Food Sci 47:457–460

    Google Scholar 

  42. Kirimi J, Musalia L, Munguti J (2017) Effect of replacing fish meal with blood meal on chemical composition of supplement for Nile tilapia (Oreochromis niloticus). East Afr Agric For J 82:1–9

    Google Scholar 

  43. Divakala K, Chiba L, Kamalakar R, Rodning S, Welles E, Cummins K, Swann J, Cespedes F, Payne R (2009) Amino acid supplementation of hydrolyzed feather meal diets for finisher pigs. J Anim Sci 87:1270–1281

    Google Scholar 

  44. Zhao W, Yang R, Zhang Y, Wu L (2012) Sustainable and practical utilization of feather keratin by an innovative physicochemical pretreatment: high density steam flash-explosion. Green Chem 14:3352–3360

    Google Scholar 

  45. Al-Rabadi GJ, Hosking BJ, Torley PJ, Williams BA, Bryden WL, Nielsen SG, Black JL, Gidley MJ (2017) Regrinding large particles from milled grains improves growth performance of pigs. Anim Feed Sci Technol 233:53–63

    Google Scholar 

  46. Bao Z, Li Y, Zhang J, Li L, Zhang P, Huang F (2016) Effect of particle size of wheat on nutrient digestibility, growth performance, and gut microbiota in growing pigs. Livest Sci 183:33–39

    Google Scholar 

  47. Neathery M, Pugh D, Miller W, Gentry R, Whitlock R (1980) Effects of sources and amounts of potassium on feed palatability and on potassium toxicity in dairy calves. J Dairy Sci 63:82–85

    Google Scholar 

  48. Bragulla HH, Homberger DG (2009) Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia. J Anat 214:516–559

    Google Scholar 

  49. Wortmann FJ, Wortmann G, Marsh J, Meinert K (2012) Thermal denaturation and structural changes of α-helical proteins in keratins. J Struct Biol 177:553–560

    Google Scholar 

  50. Ullah A, Vasanthan T, Bressler D, Elias AL, Wu J (2011) Bioplastics from feather quill. Biomacromolecules 12:3826–3832

    Google Scholar 

  51. Khurana R, Fink AL (2000) Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophys J 78:994–1000

    Google Scholar 

  52. Zhou X, Xu J, Zhao X, Zhang Z, Yao K, Liu D (2004) Spectroscopic evidence of azone effect on the keratin in mouse stratum corneum. Chem J Chinese U 25:1273–1276

    Google Scholar 

  53. Olesberg JT, Liu L, Van Zee V, Arnold MA (2006) In vivo near-infrared spectroscopy of rat skin tissue with varying blood glucose levels. Anal Chem 78:215–223

    Google Scholar 

  54. Xu W, Ke G, Wu J, Wang X (2006) Modification of wool fiber using steam explosion. Eur Polym J 42:2168–2173

    Google Scholar 

  55. Xie MX, Yuan L (2002) Studies on the hydrogen bonding of aniline’s derivatives by FT-IR. Spectrochim Acta A Mol Biomol Spectrosc 58:2817–2826

    Google Scholar 

  56. Carbonaro M, Maselli P, Nucara A (2012) Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study. Amino Acids 43:911–921

    Google Scholar 

  57. Wang H, Faris RJ, Wang T, Spurlock ME, Gabler N (2009) Increased in vitro and in vivo digestibility of soy proteins by chemical modification of disulfide bonds. J Am Oil Chem Soc 86:1093–1099

    Google Scholar 

  58. Yu P (2005) Protein secondary structures (alpha-helix and beta-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach. Br J Nutr 94:655–665

    Google Scholar 

  59. Zhang Z, Nie Y, Zhang Q, Liu X, Tu W, Zhang X, Zhang S (2017) Quantitative change in disulfide bonds and microstructure variation of regenerated wool keratin from various ionic liquids. ACS Sustain Chem Eng 5:2614–2622

    Google Scholar 

  60. Xie F, Chao Y, Yang X, Yang J, Xue Z, Luo Y, Qian S (2010) Purification and characterization of four keratinases produced by Streptomyces sp. strain 16 in native human foot skin medium. Bioresour Technol 101:344–350

    Google Scholar 

  61. Hogg PJ (2003) Disulfide bonds as switches for protein function. Trends Biochem Sci 28:210–214

    Google Scholar 

  62. Kinsella JE (1987) Physical-properties of food and milk components: research needs to expand uses. J Dairy Sci 70:2419–2428

    Google Scholar 

Download references

Funding

This work was supported by Science and Technology Plan Project of Guangdong Province (2017A020224022; 2016B090918090), Guangzhou Sci-Technology Project (201508020070), High-tech Industry and Strategically Emerging Industries Sci-Technology Project of Zhaoqing High-tech Zone (2015B010102006), the Special Program for Leading Talents of Guangdong Province (2015TX01N036), and the GDAS’ Special Project of Science and Technology Development (No. 2019GDASYL-0401002).

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  1. Lian Zhou and Xiaolin Xie contributed equally to this work.

Authors and Affiliations

  1. State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application, Guangzhou Provincial Open Laboratory of Microbial New Application Technique, Guangdong Institute of Microbiology, Guangzhou, Guangdong, China

    Lian Zhou, Xiaolin Xie, Tianfu Wu, Meibiao Chen, Honghui Zhu & Weilin Zou

  2. College of Agriculture, South China Agricultural University, Guangzhou, Guangdong, China

    Qing Yao

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  1. Lian Zhou
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  2. Xiaolin Xie
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Correspondence to Honghui Zhu.

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Zhou, L., Xie, X., Wu, T. et al. Compound enzymatic hydrolysis of feather waste to improve the nutritional value. Biomass Conv. Bioref. 12, 287–298 (2022). https://doi.org/10.1007/s13399-020-00643-y

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