Separation, Purification and Biological Activity Evaluation of Antimicrobial Peptides from Tenebrio molitor
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Abstract:
Antibacterial peptides were prepared by hydrolysis of the proteins from Tenebrio molitor using alkaline protease. The antibacterial peptides were further separated and purified. Five fractions were obtained from the dynamic adsorption of the protease hydrolysate on macroporous adsorption resin and gradient elution. Theantibacterial activity, thermostability, and molecular weight of different fractions of the peptides were compared. The antimicrobial susceptibility test indicated that the ethanol-eluted fraction exhibited the strongest antimicrobial activity. This fraction was further separated into two subfractions (H-1 and H-2) by preparative high-performance liquid chromatography (HPLC). The H-2 subfraction showed relatively strong antimicrobial activities on E. coli, Salmonella and Staphylococcus aureus, with a minimum inhibitory concentration (MIC) of 0.512 mg/mL. The thermostability tests indicated that H-2 was heat stable and could maintain a relatively strong antimicrobial activity after being heated to 121 ℃ for 20 minutes. The liquid chromatography–mass spectrometry (LC-MS) results indicated the molecular weight of H-2 was 756.82 Da. The results of this study provide a scientific basis for efficient separation and purification of antibacterial peptides from Tenebrio molitor and provide data supporting the application of antibacterial peptides from Tenebrio molitor as food preservatives.
