RESUMEN
BACKGROUND: Oxidation has been reported as the one of the deterioration reactions of proteins in aquatic products. Searching for new bioactive substances from marine algae has been one of the main areas in food science and additives. RESULTS: In this study, a novel protein from the red alga Porphyra haitanensis was determined after ammonium sulfate precipitation and gel filtration chromatography. It closely corresponded to the antioxidant activity and was identified as an uncharacterized protein with a molecular mass of 43 kDa, designated Ph43. Bioinformatic analysis revealed that Ph43 is a novel protein of non-phycobiliprotein family with putative chordin domains and rich in α-helical conformation. Recombinant protein (rPh43) was expressed in Escherichia coli as a Hig-tagged protein using a pET-22b vector system and purified by affinity high-performance liquid chromatography. Spectroscopy analysis revealed that there were no structural differences between rPh43 and natural recovered Ph43. Moreover, rPh43 showed equal/higher antioxidant activity compared with Ph43. rPh43 has the potential for application as a natural antioxidant for food stabilization. CONCLUSION: Our results identified a novel antioxidant protein with molecular mass of 43 kDa derived from Porphyra haitanensis that belongs to the non-phycobiliprotein family. © 2023 Society of Chemical Industry.