Abstract
A novel adsorbent based on peanut shells modified with glutaraldehyde and succinic anhydride was prepared. Factors affecting the adsorption capacity, such as the pH, temperature, adsorption time, initial cytochrome c (cyt c) concentration and NaCl ionic strength, were extensively investigated. The results showed that the maximum adsorption capacity of the modified peanut shells (MPSs) was 432.6 mg/g when 10 mL of cyt c solution was adsorbed by 20 mg of MPSs at pH 5.0 for 3 h. In contrast, the adsorption capacities of the unmodified peanut shells (PSs), alkaline peanut shells (APSs) and crosslinked peanut shells (CPSs) were only 100.6, 180.3, and 173.0 mg/g, respectively, 4.3-, 2.4-, and 2.5-fold lower, respectively, than that of the modified shells. The desorption rate reached 89.9% with 1.5 mol/L NaCNS as an eluent, because the electrostatic attraction between the positive charges of the protein and the negative charges of the MPSs was reduced when the ionic strength was increasing. The MPSs were used to separate and purify cytochrome c from pig myocardium. A purification of 13.5-fold in a single step with a total enzyme activity recovery of 74.0% was achieved.
Highlights
Cyt c, a type of spherical electronic-transfer protein in the biological respiratory chain that has high biological stability, is an alkaline respiratory enzyme with an iron porphyrin group but is an important cell respiration activator
The results showed that the maximum adsorption capacity of the modified peanut shells (MPSs) was 432.6 mg/g when 10 mL of cyt c solution was adsorbed by 20 mg of MPSs at pH 5.0 for 3 h
Experiments on the purification cyt c with different adsorbents have been reported. These adsorbents include polyhydroxylethyl methylacrylic acid bonded with dimethyleneimine [1], Fe3O4 containing nanomaterials modified with Cl-NH2 [2] and magnetic materials bonded with Cu2+ [3] None of these adsorbents is a biomaterial, and they all have a low adsorption capacity for cyt c
Summary
A type of spherical electronic-transfer protein in the biological respiratory chain that has high biological stability, is an alkaline respiratory enzyme with an iron porphyrin group but is an important cell respiration activator. It is readily soluble in water and acidic solutions and is abundant in yeast and animal myocardium. Crude cyt c is obtained from animal myocardium by salting-out and further purified by column chromatography This process is time consuming and has a low throughput. The affinities of peanut shells for cyt c differ based on the modified group. Using optimised parameters, cyt c was purified from a solution crude extract of pig myocardium using this novel adsorbent
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