蛋清蛋白质降压肽纯化及分子量测定  

Purification and molecular weight assay of antihypertensive peptides derived from egg white protein

作　　者：于志鹏[1] 赵文竹[1] 于一丁[1] 刘静波[1] 

机构地区：[1]吉林大学军需科技学院营养与功能食品研究室,吉林长春130062

出　　处：《食品工业科技》2010年第7期230-232,共3页Science and Technology of Food Industry

基　　金：国家高技术研究发展计划(863)项目(2007AA10Z329)

摘　　要：蛋清蛋白质Alcalase2.4L酶解产物经交联葡聚糖凝胶Sephadex G-25纯化,去离子水洗脱,采用体外检测方法筛选具有血管紧张素转化酶抑制作用的高活性组分。利用高效凝胶过滤色谱（GPC）方法测定纯化高活性组分的分子量分布,根据马尿酸、Gly-Gly-Gly、Gly-Gly-Tyr-Arg和杆菌肽四种标准品的分子量对数与出峰时间的关系,运用GPC软件,绘制标准分子量分布的标准曲线。结果表明：纯化的各个组分中,洗脱时间在180-190min的组分抑制率最高（83.18%）,高活性组分的IC50=0.18mg/mL,经GPC测定其分子量分布为241.2198-509.6793Da.The antihypertensive peptides derived from egg white protein were purified by Sephadex G-25.High activity fraction was screened by determining the angiotensin converting enzyme inhibitory property in vitro,and the molecular weight was measured by GPC. The molecular weight distribution curve was obtained as the relationship between molecular weight and elution time. The results showed that the fraction of eluted at time 180-190min had high angiotensin converting enzyme inhibitory activity which was 83.18%,the value of IC50 0.18mg/mL,molecular weight distribution as 241.2198-509.6793Da.

关 键 词：蛋清蛋白质 肽 降血压 纯化 

分 类 号：TS201.21[轻工技术与工程—食品科学]