乳铁蛋白水解物修饰物的分离纯化及其抗大肠杆菌活性研究

马春敏; 薄力影; 范婧; 李铁晶

doi:10.13386/j.issn1002-0306.2018.01.017

乳铁蛋白水解物修饰物的分离纯化及其抗大肠杆菌活性研究

Isolation and purification of lactoferrinhydrolysate's modifier and determination of its antibacterial activity on Escherichia coli

摘要

摘要: 利用胃蛋白酶水解乳铁蛋白得到最小抑菌浓度为200 mg/mL的乳铁蛋白水解物(LHS),进行类蛋白反应导入色氨酸(Trp)得到乳铁蛋白水解物修饰物。对LHS及其色氨酸修饰产物采用Sephadex G-25进行分离纯化,收集出峰产物,比较各级产物的抗大肠杆菌活性。结果表明,LHS和Trp修饰物分离纯化后的峰1为抑菌活性峰,各级产物的抑菌效果为LHS

Abstract: The lactoferrinhydrolysate(LHS)with a minimum inhibitory bacterial concentration of 200 mg/mL was hydrolyzed by pepsin. And then the lactoferrinhydrolysate was modified with tryptophan(Trp)LHS and its tryptophan modifier were separated and purified by Sephadex G-25. The peak products were collected and their antibacterial activity was determined. Especially, the purred peak 1 belong to the antibacterial activity peak and the antibacterial effect of the separative products were LHSEscherichia coli were 40.42% and 85.83% at the concentration of 200 mg/mL. When adding the concentration of 100 mg/mL, the inhibitory rates of LHS's peak 1 product, Trp modifier and Trp modifier's peak 1 product on Escherichia coli were 41.12%, 58.31% and 88.00%, respectively. Then, the inhibition rate of tryptophan modifier against Escherichia coli was 45.41% higher than its unmodifier. The inhibition rate of tryptophan modifier's purified product against Escherichia coli was 29.69% higher than its not purified product. The collected products were further separated and identified by reversed-phase high performance liquid chromatography(HPLC).The result demonstrated that the antibacterial peptide with high purity and high activity was obtained by separation and purification.

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