裸燕麦球蛋白酶解液的纯化及其抗氧化研究  

Preparation of Antioxidant Peptides from Naked Oat Globulin by Alkaline Protease Hydrolysis

作　　者：张美莉[1] 蔺瑞[1] 管文荻[1] 马萨日娜[1] 

机构地区：[1]内蒙古农业大学食品科学与工程学院,内蒙古呼和浩特010018

出　　处：《食品科学》2011年第15期113-116,共4页Food Science

基　　金：国家自然科学基金项目(30960240);内蒙古自然科学基金项目(2009MS0307)

摘　　要：通过Osborne法制得的裸燕麦球蛋白,利用碱性蛋白酶对其进行酶解,采用Sephadex G-25凝胶层析对酶解液进行纯化及其分子质量测定,然后对各分离组分清除.OH、O-2.、DPPH自由基能力进行研究。结果表明:酶解液经分离纯化得到图谱为2个峰,分别为组分I(分子质量10738～133929D)和组分II(分子质量114～861D)。测得组分II清除.OH(IC50 0.589mg/mL)、O-2.(IC50 1.783mg/mL)、DPPH自由基(IC50 0.095mg/mL)能力高于组分I和酶解液。Naked oat globulin was prepared by Osborne,s method and hydrolyzed by alkaline protease.The antioxidant peptides in the hydrolysate were purified by Sephadex G-25 gel filtration chromatography and their molecular weights were determined.The scavenging capacity of each purified fraction against hydroxyl,superoxide anion and DPPH free radicals was also determined.The results indicated that two fractions were obtained from hydrolyzed naked oat globulin and named as fraction I and fraction II.The molecular weight ranges of fraction I and fraction II were 10738-133929 and 114-861 D,respectively.In addition,fraction II had higher scavenging effect against hydroxyl radicals（IC50 = 0.589 mg/mL）,superoxide anion radicals（IC50 = 1.783 mg/mL） and DPPH radicals（IC50 = 0.095 mg/mL） than fraction I and the hydrolysate.

关 键 词：碱性蛋白酶 裸燕麦 球蛋白 抗氧化 活性肽 

分 类 号：TS201.25[轻工技术与工程—食品科学]