Abstract
Bovine hemoglobin is the major component of the cruor (slaughterhouse by-product) and can be considered as an important source of active peptides that could be obtained by pepsic hydrolysis. The kinetics of appearance and disappearance of several antibacterial peptides from α 1–32 family during hydrolysis of synthesized α 1–32 peptide, of purified bovine hemoglobin and of cruor was studied, and reaction scheme for the hydrolysis of α 1–32 family peptides from these three sources was determined. On this basis, a mathematical model was proposed to predict the concentration of each peptide of interest of this family depending on hydrolysis time, and also on temperature (in the range 15–37 °C), pH (in the range 3.5–5.5) and enzyme to substrate ratio (in the range 1/50–1/200 for the synthesized peptide and 1/5–1/20 for purified bovine hemoglobin and cruor). Apparent rate constants of reactions were determined by applying the model on a set of experimental data and it was shown that they depended on the temperature according to Arrhenius’s law, that their dependence on the pH was linear, and that enzyme to substrate ratio influence was limited (in the studied range).
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Hedhili, K., Dimitrov, K., Vauchel, P. et al. Valorization of cruor slaughterhouse by-product by enzymatic hydrolysis for the production of antibacterial peptides: focus on α 1–32 family peptides mechanism and kinetics modeling. Bioprocess Biosyst Eng 38, 1867–1877 (2015). https://doi.org/10.1007/s00449-015-1427-2
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DOI: https://doi.org/10.1007/s00449-015-1427-2