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Biosorption/Precipitation of Heavy Metals by Partially Degraded Keratin/Soluble Peptides/Amino Acids By-Products of Degradation of Human Hair by Keratinase Isolated from Alcaligenes Faecalis Strain AIR10

Ezenwali Moses Obinna(1),


(1) Enugu State University of Science and Technology
Corresponding Author

Abstract


This research involves a systematic process to reduce the effects of heavy metals on health and the environment through the metabolism of human hair. In this study, the by-product of the breakdown of microbial keratinase was keratin; free amino acids and partially degraded peptide/keratin were used as precipitates and adsorbents, respectively, to remove Copper (Cu), Iron (Fe), Nickel (Ni), Zinc (Zn) Cobalt (Co) and Lead (Pb) from pollution. Atomic absorption spectrophotometry is used to measure metal concentrations. Degraded human hair was an efficient but insignificant weight absorber compared to untreated human hair, achieving almost 85.81±0.0077% adsorption for chloride. Our data show that alkaline pH favors lead acetate deposited by the supernatant over neutral and acidic regions. Both treated and untreated human hair showed a significant percentage of ZnSO4 and NiCl2 biosorption, with CuSO4 showing the percentage of precipitation, the lowest percentage of biosorption. Our SEM results suggest that a technology may be required to increase the surface area of treated human hair to increase the adsorption capacity.

Keywords


AIR10; Biosorption; Degraded keratin; Hair

References


Anand, C., Mehta, M., and Shah, G. (1992). Degradation of keratin waste products by Kocuria rosea. Microbiology, 58, 3271-3275.

Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science, 181, 223-230.

Brandelli, A., and Riffel, A. (2005). Production of an extracellular keratinase from Chryseobacterium sp. growing on raw feathers. Electronic Journal of Biotechnology, 8(1), 35-42.

De Toni, C., Richter, M., Chagas, J., Henriques, J. A., and Termignoni, C. (2002). Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophilia strain. Canadian Journal of Microbiology, 48(4), 342-348.

Dhiva, S., Ranjith, K., Prajisya, P., Sona, K., Narendrakumar, G., Prakash, P., Emilin Renitta, R., and Samrot, A. V. (2020). Optimization of keratinase production using Pseudomonas aeruginosa Su-1 having feather as substrate. Biointerface Research in Applied Chemistry, 10, 6540-6549.

Dill, K.A. (1990) Dominant forces in protein folding. Biochemistry, 29, 7133-7155.

Genchi, G., Sinicropi, M. S., Lauria, G., Carocci, A., and Catalano, A. (2020). The effects of cadmium toxicity. International Journal of Environmental Research and Public Health, 17(11), 3782.

Jankiewicz, U., and Frąk, M. (2017). Identification and properties of a keratinase from Stenotrophomonas maltophilia N4 with potential application in biotechnology. Ecological Questions, 28, 15-24.

Kani, T., Subha, K., Madhanraj, P., Senthilkumar, G., and Panneerselvam, A. (2012). Degradation of chicken feathers by Leuconostoc sp. and Pseudomonas microphilus. European Journal of Experimental Biology, 2(2), 358-362.

Klink, T. A., Woycechowsky, J. K., Kimberly, M. T., and Raines, T. R. (2000). Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. European Journal of Biochemistry, 267, 566-572.

Lee, E. (2017). Emerging roles of protein disulfide isomerase in cancer. BMB reports, 50(8), 401.

Mazotto, A., Lage Cedrola, S., Lins, U., Rosado, A., Silva, K., Chaves, J., Rabinovitch, L., Zingali, R., and Vermelho, A. (2010). Keratinolytic activity of Bacillus subtilis AMR using human hair. Letters in Applied Microbiology, 50(1), 89-96.

Mendonça, F. G., Silva, T. G., Nascimento, G. M. d., Stumpf, H. O., Mambrini, R. V., and Pim, W. D. d. (2019). Human hair as adsorbent of palladium (II) in solution: a precursor of well-dispersed size-controlled Pd nanoparticles. Journal of the Brazilian Chemical Society, 30, 736-743.

Nnolim, N. E., Mpaka, L., Okoh, A. I., and Nwodo, U. U. (2020). Biochemical and molecular characterization of a thermostable alkaline metallo-keratinase from Bacillus sp. Nnolim-K1. Microorganisms, 8(9), 1304.

Obinna, E. M. (2022). Physicochemical properties of human hair using Fourier transform infra-red (FTIR) and scanning electron microscope (SEM). ASEAN Journal of Science and Engineering in Materials, 1(2), 71-74.

Park, G.-T., and Son, H.-J. (2009). Keratinolytic activity of Bacillus megaterium F7-1, a feather-degrading mesophilic bacterium. Microbiological research, 164(4), 478-485.

Putnam, F. W., and Neurath, H. (1944). The Precipitation of Proteins by Synthetic Detergents1a. Journal of the American Chemical Society, 66(5), 692-697.

Sharaf, E. F., and Khalil, N. M. (2011). Keratinolytic activity of purified alkaline keratinase produced by Scopulariopsis brevicaulis (Sacc.) and its amino acids profile. Saudi Journal of Biological Sciences, 18(2), 117-121.

Sharma, R., and Rajak, R. C. (2003). Keratinophilic fungi: Nature’s keratin degrading machines! Resonance, 8(9), 28-40.

Singh, S., Shrivastava, A. R., Gupta, A., Singh, A. K., Gopalan, N., and Chaudhary, H. S. (2012). Keratinloytic Actinomycetes isolated from poultry waste. Journal of Chemical and Pharmaceutical Research, 4(9), 4107-4111.

Tridico, S. R., Koch, S., Michaud, A., Thomson, G., Kirkbride, K. P., and Bunce, M. (2014). Interpreting biological degradative processes acting on mammalian hair in the living and the dead: which ones are taphonomic? Proceedings of the Royal Society B: Biological Sciences, 281(1796), 20141755.

Wiedemann, C., Kumar, A., Lang, A., and Ohlenschläger, O. (2020). Cysteines and disulfide bonds as structure-forming units: insights from different domains of life and the potential for characterization by NMR. Frontiers in Chemistry, 8, 280.


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