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The simultaneous production of single-cell protein and a recombinant antibacterial peptide by expression of an antibacterial peptide gene in Yarrowia lipolytica






Process Biochemistry 48(2): 212-217

The simultaneous production of single-cell protein and a recombinant antibacterial peptide by expression of an antibacterial peptide gene in Yarrowia lipolytica

In this study, the DNA fragment encoding the N-terminus of scallop H2A was expressed in the marine-derived yeast Yarrowia lipolytica, which has a high protein content. After cultivation in PBB medium for 120h, the transformant producing the highest amount of antibacterial peptide, 29a, was obtained. The supernatant from cultures of 29a had killing activity against Vibrio harveyi, V. anguillarum, and V. parahaemolyticus. After purification, the molecular mass of the recombinant antibacterial peptide was 4.5kDa, and the purified recombinant antibacterial peptide was able to cause leakage of intracellular components from both whole and protoplast cells of V. parahaemolyticus. The results indicated that when the yeast transformant 29a was grown in YPD medium, PBB medium or hydrolysate of soybean meal containing ammonium sulfate, its cells still had a high protein content. Because this recombinant marine yeast both had a high protein content and produced the antibacterial peptide, it has high value-added applications. The DNA fragment encoding the N-terminus of scallop H2A was expressed in the marine derived Yarrowia lipolytica. The transformant 29a had the antibacterial activity against Vibrio spp and high protein content. The molecular mass of the recombinant antibacterial peptide was 4.5kDa. The purified recombinant antibacterial peptide could cause leakage of the bacteria.

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Accession: 036731379

DOI: 10.1016/j.procbio.2013.01.003



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