Characterization of recombinant protein ferritin from Pyropia yezoensis (rPyFer) and its biological activities
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Characterization of recombinant protein ferritin from Pyropia yezoensis (rPyFer) and its biological activities Selvakumari Ulagesan1 • Jeong-Wook Choi1 • Taek-Jeong Nam1 • Youn-Hee Choi1,2
Received: 4 March 2020 / Revised: 9 August 2020 / Accepted: 31 August 2020 / Published online: 6 October 2020 Ó The Korean Society of Food Science and Technology 2020
Abstract Ferritins are iron-binding proteins that are basically participated in iron storage, detoxification, and immune response. In the present study, ferritin gene from the marine red algae Pyropia yezoensis was cloned into a pET21d expression vector. High-efficiency transformation was performed in Escherichia coli BL21, the recombinant protein was expressed by induction with 0.1 mM isopropyl-b-D-thiogalactoside and purified via ammonium sulfate precipitation, anion exchange and size exclusion chromatography. The purified recombinant ferritin from P. yezoensis (rPyFer) was characterized and analyzed for its antimicrobial activity against both Gram-negative and Gram-positive bacterial cultures and exhibited significant antibacterial activity against Gram-positive cultures. The recombinant protein was also analyzed for its iron-uptake and radical-scavenging activities; rPyFer exhibited significant iron-uptake activity at low concentrations, and its radical-scavenging activity increased in a dose-dependent manner. This research will contribute to the development of new therapeutic proteins from marine algae.
& Youn-Hee Choi [email protected] Selvakumari Ulagesan [email protected] Jeong-Wook Choi [email protected] Taek-Jeong Nam [email protected] 1
Institute of Fisheries Sciences, Pukyong National University, Busan 46041, Republic of Korea
2
Department of Marine Bio-materials and Aquaculture, Pukyong National University, 45, Yongso-ro, Nam-Gu, Busan 48513, Republic of Korea
Keywords Recombinant protein Pyropia yezoensis Ferritin Equine spleen ferritin Marine algae Antioxidant activity Minimum inhibitory concentration
Introduction Ferritin is an important iron-binding protein which is found in all species. Ferritin is made up of a hollow spherical oligomer consisting of 24 subunits, and iron can be stored within this structure as stable and nontoxic state to fulfil iron requirements (Arosio et al., 2009). In vertebrates, ferritin composed of two homologous subunits, light (L)ferritin and heavy (H)-ferritin, they have different specialized roles. H-ferritin exhibits ferroxidase activity and participates in rapid iron uptake and detoxification, whereas L-ferritin is involved in long-term iron storage (Ford et al., 1984). Algae was confirmed to be an excellent source of iron for supplementation. Several types of marine macroalgae are commonly consumed in countries such as Korea, Japan, and China. Among these macroalgae, the red alga P. yezoensis, also called nori, is the most important species and contains high levels of iron, zinc, and manganese, as well as folic acid and vitamins A, B12 and C (Takatoshi and Miho, 1993). Although the iron content of
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