Biotechnology and Bioprocess Engineering

, Volume 14, Issue 1, pp 84–90 | Cite as

Amino acid and soluble protein cocktail from waste keratin hydrolysed by a fungal keratinase of Paecilomyces marquandii

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Abstract

Waste bovine hooves and horns were enzymatically hydrolysed into soluble products intended for foliar fertilizer. With the powdered keratin at 50°C and pH 8 between 34 to nearly 60% of nitrogen was solubilized in 5 h, depending on the enzyme concentration. The reaction could further be improved by steam pretreatment of the keratin, resulting in 98% solubilisation of the nitrogen. The products of hydrolysis consisted of a mixture of soluble proteins, peptides, and free amino acids. Among the latter, 18 common amino acids were detected. Several of them were previously recognized to have a positive effect on plants. Nonpolar neutral, basic, and sulphur amino acids were present in relatively large amounts, while proline and tryptophan were not found. Comparison with other protein hydrolysates aimed for fertilizer suggests that keratin degradation products, obtained by enzymatic hydrolysis, have potential to be used for foliar fertilization, alone or in a combination with another complementary hydrolysate of a different source, such as skin or plant proteins.

Keywords

keratinous waste waste bioconversion keratin hydrolysis fungal keratinase Paecilomyces marquandii foliar plant fertilizer 
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References

  1. 1.
    Wainwright, M., W. Nevell, and U. Skiba (1985) Fertilizer potential of some commercially available forms of keratin microbial biomass. Enzyme Microb. Technol. 7: 108–110.CrossRefGoogle Scholar
  2. 2.
    Chapin, F. S., L. Moilanen, and K. Kielland (1993) Preferential use of organic nitrogen for growth by a nonmycorrhizal arctic sedge. Nature 361: 150–153.CrossRefGoogle Scholar
  3. 3.
    Endres, L. and H. Mercier (2003) Amino acid uptake and profile in bromeliads with different habits cultivated in vitro. Plant Physiol. Biochem. 41: 181–187.CrossRefGoogle Scholar
  4. 4.
    Cavani, L., C. Ciavatta, and C. Gessa (2003) Determination of free L- and D- alanine in hydrolysed protein fertilizers by capillary electrophoresis. J. Chromatogr. A 985: 463–469.CrossRefGoogle Scholar
  5. 5.
    Ashmead, H. D., H. H. Ashmead, G. W. Miller, and H. H. Hsu (1986) Foliar Feedings of Plants with Amino Acid Chelates. 1st ed., pp. 370. Noyes Publications, Park Ridge, NJ, USA.Google Scholar
  6. 6.
    Nagao, K., M. Takeuchi, Y. Miyazawa, H. Sato, H. O. Yokota, and K. Kita (2005) Foliar application of fertilizer based on proline and inosine stimulates the second flush growth of Italian ryegrass (Lolium multiflorum Lam.). Grassl. Sci. 51: 269–270.CrossRefGoogle Scholar
  7. 7.
    Attoa, G. E., H. E. Wahba, and A. A. Farahat (2002) Effect of some amino acids and sulphur fertilization on growth and chemical composition of Iberis amara L. plants. Egypt. J. Hort. 29: 17–37.Google Scholar
  8. 8.
    Furuya, S. and Y. Umemiya (2002) The influence of chemical forms on foliar-applied nitrogen absorption for peach trees. Acta Hort. 594: 97–103.Google Scholar
  9. 9.
    Koksal, A. I., H. Dumanoglu, N. T. Gunes, and M. Aktas (1999) The effects of different amino acid chelate foliar fertilizers on yield, fruit quality, shoot growth and Fe, Zn, Cu, Mn content of leaves in Williams pear cultivar (Pyrus communis L.). Turk. J. Agric. For. 23: 651–658.Google Scholar
  10. 10.
    Suzuki, Y., Y. Tsujimoto, H. Matsui, and K. Watanabe (2006) Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria. J. Biosci. Bioeng. 102: 73–81.CrossRefGoogle Scholar
  11. 11.
    Farag, A. M. and M. A. Hassan (2004) Purification, characterization and immobilization of a keratinase from Aspergillus oryzae. Enzyme Microb. Technol. 34: 85–93.CrossRefGoogle Scholar
  12. 12.
    Williams, C. M., C. G. Lee, J. D. Garlich, and J. C. H. Shih (1991) Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein. Poult. Sci. 70: 85–94.Google Scholar
  13. 13.
    Ichida, J. M., L. Krizova, C. A. LeFevre, H. M. Keener, D. L. Elwell, and E. H. Burtt, Jr. (2001) Bacterial inoculum enhances keratin degradation and biofilm formation in poultry compost. J. Microbiol. Methods 47: 199–208.CrossRefGoogle Scholar
  14. 14.
    Grazziotin, A., F. A. Pimentel, S. Sangali, E. V. de Jong, and A. Brandelli (2007) Production of feather protein hydrolysate by keratinolytic bacterium Vibrio sp. kr2. Bioresour. Technol. 98: 3172–3175.CrossRefGoogle Scholar
  15. 15.
    Moreira, F. G., C. G. M. de Souza, M. A. F. Costa, S. Reis, and R. M. Peralta (2007) Degradation of keratinous materials by the plant pathogenic fungus Myrothecium verrucaria. Mycopathologia 163: 153–160.CrossRefGoogle Scholar
  16. 16.
    Kida, K., S. Morimura, J. Noda, Y. Nishida, T. Imai, and M. Otagiri (1995) Enzymatic hydrolysis of the horn and hoof of cow and buffalo. J. Ferment. Bioeng. 80: 478–484.CrossRefGoogle Scholar
  17. 17.
    Gupta, R. and P. Ramnani (2006) Microbial keratinases and their prospective applications: an overview. Appl. Microbiol. Biotechnol. 70: 21–33.CrossRefGoogle Scholar
  18. 18.
    Friedrich, J., H. Gradišar, D. Mandin, and J. P. Chaumont (1999) Screening fungi for synthesis of keratinolytic enzymes. Lett. Appl. Microbiol. 28: 127–130.CrossRefGoogle Scholar
  19. 19.
    Anbu, P., S. C. B. Gopinath, A. Hilda, N. Mathivanan, and G. Annadurai (2006) Secretion of keratinolytic enzymes and keratinolysis by Scopulariopsis brevicaulis and Trichophyton mentagrophytes: regression analyses. Can. J. Microbiol. 52: 1060–1069.CrossRefGoogle Scholar
  20. 20.
    Lin, X., C. G. Lee, E. S. Casale, and J. C. H. Shih (1992) Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain. Appl. Environ. Microbiol. 58: 3271–3275.Google Scholar
  21. 21.
    Atalo, K. and B. A. Gashe (1993) Protease production by a thermophilic Bacillus species (P-001A) which degrades various kinds of fibrous proteins. Biotechnol. Lett. 15: 1151–1156.CrossRefGoogle Scholar
  22. 22.
    Giongo, J. L., F. S. Lucas, F. Casarin, P. Heeb, and A. Brandelli (2007) Keratinolytic proteases of Bacillus species isolated from the Amazon basin showing remarkable de-hairing activity. World J. Microbiol. Biotechnol. 23: 375–382.CrossRefGoogle Scholar
  23. 23.
    Böckle, B., B. Galunsky, and R. Müller (1995) Characterisation of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530. Appl. Environ. Microbiol. 61: 3705–3710Google Scholar
  24. 24.
    Letourneau, F., V. Soussotte, P. Bressollier, P. Branland, and B. Verneuil (1998) Keratinolytic activity of Streptomyces sp. S.K1-02: a new isolated strain. Lett. Appl. Microbiol. 26: 77–80.CrossRefGoogle Scholar
  25. 25.
    Chao, Y. P., F. H. Xie, J. Yang, J. H. Lu, and S. J. Qian (2007) Screening for a new Streptomyces strain capable of efficient keratin degradation. J. Environ. Sci. 19: 1125–1128.CrossRefGoogle Scholar
  26. 26.
    Onifade, A. A., N. A. Al-Sne, A. A. Al-Musallam, and S. Al-Zarban (1998) A review: potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources. Bioresour. Technol. 66: 1–11.CrossRefGoogle Scholar
  27. 27.
    Gradišar, H., J. Friedrich, I. Križaj, and R. Jerala (2005) Similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases. Appl. Environ. Microbiol. 71: 3420–3426.CrossRefGoogle Scholar
  28. 28.
    Friedrich, J., H. Gradišar, M. Vrecl, and A. Pogačnik (2005) In vitro degradation of porcine skin epidermis by a fungal keratinase of Doratomyces microsporus. Enzyme Microb. Technol. 36: 455–460.CrossRefGoogle Scholar
  29. 29.
    Davídek, J., J. Hrdlička, M. Karvánek, J. Pokorný, J. Seifert, and J. Velíšk (1977) Laboratorní Příručka Analýzy Potravin. 1st ed., pp. 720. SNTL, Prague, Czech Republic.Google Scholar
  30. 30.
    Hublin, A., H. Gradišar, J. Friedrich, and D. Vasić-Rački (2002) Stability and stabilization of Doratomyces microsporus keratinase. Biocatal. Biotransformation 20: 329–336.CrossRefGoogle Scholar
  31. 31.
    Wiechelman, K. J., R. D. Braun, and J. D. Fitzpatrick (1988) Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal. Biochem. 175: 231–237.CrossRefGoogle Scholar
  32. 32.
    Kurbanoglu, E. B. and O. F. Algur (2002) The influence of ram horn hydrolyzate on the crop yield of the mush-room Agaricus bisporus. Sci. Hortic. 94: 351–357.CrossRefGoogle Scholar
  33. 33.
    Sorimachi, K., T. Okayasu, K. Akimoto, and A. Niwa (2000) Conservation of the basic pattern of cellular amino acid composition during biological evolution in plants. Amino Acids 18: 193–197.CrossRefGoogle Scholar
  34. 34.
    Parrado, J., J. Bautista, E. J. Romero, A. M. García-Martínez, V. Friaza, and M. Tejada (2008) Production of a carob enzymatic extract: potential use as a biofertilizer. Bioresour. Technol. 99: 2312–2318CrossRefGoogle Scholar
  35. 35.
    Bhaskar, N., V. K. Modi, K. Govindaraju, C. Radha, and R. G. Lalitha (2007) Utilization of meat industry by products: protein hydrolysate from sheep visceral mass. Bioresour. Technol. 98: 388–394.CrossRefGoogle Scholar
  36. 36.
    Bhaskar, N., T. Benila, C. Radha, and R. G. Lalitha (2008) Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease. Bioresour. Technol. 99: 335–343.CrossRefGoogle Scholar
  37. 37.
    Ohba, R., T. Deguchi, M. Kishikawa, S. Morimura, and I. Suzuki (2003) Antioxidative effect of enzymatic hydrolysate of horn and hoof in rat. Food Sci. Technol. Res. 9: 152–154.CrossRefGoogle Scholar

Copyright information

© The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg GmbH 2009

Authors and Affiliations

  1. 1.Faculty of ChemistryBrno University of TechnologyBrnoCzech Republic
  2. 2.Department of BiotechnologyNational Institute of ChemistryLjubljanaSlovenia

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