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Isolation and characterization of an antibacterial peptide from protein hydrolysates of Spirulina platensis
- Sun, Yijun, Chang, Rong, Li, Qingye, Li, Bosheng
- European food research & technology 2016 v.242 no.5 pp. 685-692
- Escherichia coli, Spirulina platensis, Staphylococcus aureus, amino acid sequences, amino acids, anti-infective agents, antimicrobial peptides, food research, hemolysis, hydrolysates, minimum inhibitory concentration, molecular weight, papain, protein hydrolysates, reversed-phase high performance liquid chromatography, spectrometers
- An antibacterial peptide SP-1 has been isolated from the alkaline protease and papain hydrolysate of Spirulina platensis through a series of chromatographic methods including Sephadex G-25 chromatography, reversed-phase high-performance liquid chromatography (RP-HPLC), and Superdex 75 10/300 GL chromatography. Its amino acid sequence was determined via liquid chromatography–tandem mass spectrometer (LC-MS/MS). SP-1 contained 18 amino acid residues (KLVDASHRLATGDVAVRA) with the molecular mass of 1878.97 Da. The minimum inhibitory concentration of SP-1 was 8 mg/mL for Escherichia coli and 16 mg/mL for Staphylococcus aureus. The hemolysis result showed that the peptide was non-toxic. Based on all these features, the Spirulina peptides can be considered to be potential promising antimicrobial agents. SP-1 is the first antibacterial peptide derived from S. platensis protein hydrolysates.