华重楼内生菌抗菌肽的分离纯化及其特性

Purification and characterization of an antimicrobial peptide from Paris polyphylla var.chinensis

摘要:

摘要：【目的】华重楼内生菌PCE45具有较强的抗菌活性，本文将对PCE45产生的抗菌物质进行分离纯化和性质分析报道。【方法】PCE45发酵液经硫酸铵盐析、丙酮沉淀、SephadexG75柱、DE52纤维素柱和SephadexG25凝胶柱纯化分离得到抗菌肽PCP-1。【结果】稳定性测试表明该抗菌肽对蛋白酶不敏感，对高温、强酸、强碱有较好的耐受性，可造成稻瘟病菌菌丝畸形并抑制孢子萌发。抑菌谱表明该抗菌肽对玉米弯胞病菌等真菌和大肠杆菌等细菌有较强的抑菌效果。质谱测得其分子量为1058.3D。氨基酸组成分析表明该

Abstract:

Abstract: [Objective] We isolated an endophyte PCE45 from the rhizome of Paris polyphylla var. chinensis. From PCE45, we purified and characterized an antimicrobial peptide. [Methods] After ammonium sulfate salting-out, acetone precipitation, SephadexG75,DE52 and SephadexG25 column chromatography, we separated an antimicrobial peptide PCP-1 from the strain PCE45. The stability against high temperature and proteinase, and antimicrobial activity were also analyzed. [Results] The antimicrobial peptide PCP-1 was stable to proteinase and tolerated high temperature, strong acid and strong base. PCP-1 caused deformation of the hyphae of Pyricularia oryzae and prohibited the spore germination. It also inhibited fungi such as Curvularia lunata and bacteria such as Escherichia coli. Mass spectrogram measurement revealed its molecular weight of 1058.3 Da. The amino acid composition of the peptide composed of 7 amino acids. Ninhydrin reaction showed negative trait whereas after acid hydrolysis with positive ninhydrin reaction and biuret reaction. [Conclusion] The ninhydrin reaction and biuret reaction imply that the peptide PCP-1 is a cyclic lipeptide. This is the first report about antimicrobial peptide from Paris polyphylla var.chinensis.