火麻仁黄嘌呤氧化酶抑制肽的分离鉴定与分子对接研究  

Study on Isolation,Identification and Molecular Docking of Xanthine Oxidase Inhibitory Peptide from Hemp Seed

作　　者：魏连会[1] 石杰[1] 张正海[1] 董艳[1] WEI Lianhui;SHI Jie;ZHANG Zhenghai;DONG Yan(Daqing Branch of the Heilongjiang Academy of Sciences,Daqing 163319)

机构地区：[1]黑龙江省科学院大庆分院,大庆163319

出　　处：《食品工业》2023年第9期301-305,共5页The Food Industry

基　　金：功能食品工程技术领军人才梯队建设项目(RC2022DQ01);黑龙江省科学院对外合作项目(HZ2022-04);黑龙江省科学院院长基金项目(YZ2023DQ01);黑龙江省省属科研院所科研业务费项目(CZKYF2021-2-B015)。

摘　　要：建立一种快速、准确筛选火麻蛋白酶解物中活性多肽的方法。在黄嘌呤氧化酶抑制活性导向下,以超滤技术与离子交换法对火麻蛋白酶解物进行分离,确定黄嘌呤氧化酶抑制活性多肽,通过质谱分析与已有序列比对的方法,确定活性多肽的氨基酸序列;通过计算机模拟将多肽与黄嘌呤氧化酶蛋白对接,筛选活性多肽,并确定其与黄嘌呤氧化酶蛋白的作用位点。共鉴定302个多肽,其中AFNVDSETVK和KTNDNAWVSPLAG这2个多肽能与黄嘌呤氧化酶稳定结合。基于串联质谱与分子对接技术,建立从混合多肽中快速筛选、鉴定活性多肽的方法,明确活性多肽与黄嘌呤氧化酶可能的结合位点,为后续的深入研究提供了依据和参考。Establish a rapid and accurate method for screening active peptides in the hydrolyzate of hemp protease.Under the guidance of xanthine oxidase inhibitory activity,ultrafiltration technology and ion exchange method were used to separate the hydrolysates of xanthine oxidase inhibitory activity polypeptide,and the amino acid sequence of the active polypeptide was determined by mass spectrometry analysis and comparison with existing sequences.Peptides were docked to xanthine oxidase protein by computer simulation,active peptides were screened,and their sites of action with xanthine oxidase protein were determined.A total of 302 peptides were identified,among which AFNVDSETVK and KTNDNAWVSPLAG could bind to xanthine oxidase stably.Based on tandem mass spectrometry and molecular docking technology,a method for rapid screening and identification of active peptides from mixed peptides was established,and the possible binding sites of active peptides and xanthine oxidase were identified,which provided basis and reference for further research.

关 键 词：火麻蛋白 黄嘌呤氧化酶抑制肽 分子对接 

分 类 号：TS201.2[轻工技术与工程—食品科学]