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-β-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.

铁蛋白是铁结合蛋白，主要参与铁的储存、解毒和免疫反应。在本研究中，来自海洋红藻Pyropia yezoensis 的铁蛋白基因被克隆到 pET21d 表达载体中。在大肠杆菌BL21 中进行高效转化，重组蛋白通过 0.1 mM 异丙基-β-D-硫代半乳糖苷诱导表达，并通过硫酸铵沉淀、阴离子交换和尺寸排阻色谱纯化。条斑紫菜的纯化重组铁蛋白(rPyFer) 被表征和分析其对革兰氏阴性和革兰氏阳性细菌培养物的抗菌活性，并对革兰氏阳性培养物表现出显着的抗菌活性。还分析了重组蛋白的铁吸收和自由基清除活性；rPyFer 在低浓度下表现出显着的铁吸收活性，其自由基清除活性以剂量依赖性方式增加。这项研究将有助于从海藻中开发新的治疗蛋白质。