摘要
采用超滤法从水飞蓟蛋白酶解物中初步分离纯化抗氧化活性肽,考察操作压力、操作温度及酶解物质量分数对超滤过程中膜通量的影响,并对超滤前后水飞蓟蛋白酶解物的抗氧化活性进行比较。结果表明:采用截留相对分子质量5 000的聚醚砜膜对水飞蓟蛋白酶解物进行超滤分离的最适工艺条件为操作压力0.1 MPa、操作温度25℃、酶解物质量分数2%;抗氧化试验显示,水飞蓟蛋白酶解物对DPPH自由基和羟基自由基的半数抑制浓度(IC50)分别由超滤前的1.34和9.71 g/L下降到1.01和5.95 g/L,超滤后蛋白酶解物螯合Fe2+的能力也有所提高,当质量浓度为2.0 g/L时,其对Fe2+的螯合率达到了37%。由此证明超滤可有效提高水飞蓟蛋白酶解物的抗氧化活性。
The ultrafiltration method for preliminary separation and purification of peptide with antioxidant activity from Silybum marianum protein hydrolysates was studied.The effects of pressure,temperature,concentration of hydrolysates on membrane flux were investigated.The antioxidant activity of Silybum marianum protein hydrolysates before ultrafiltration was compared with that after ultrafiltration.The results showed that the optimum conditions of ultrafiltration were concentration of hydrolysates 2 %,pressure of 0.1 MPa,and temperature of 25 ℃.The results of antioxidation showed that the half inhibitory concentration（IC50） value of the Silybum marianum protein hydrolysates for scavenging ·DPPH and ·OH decreased from 1.34 and 9.71 g/L to 1.01 and 5.95 g/L respectively through ultrafiltration,and the chelating rate on ferrous ions of Silybum marianum protein hydrolysates（2.0 g/L） is increased to 37% after ultrafiltration.The results confirmed that the antioxidant activity of Silybum marianum protein hydrolysates was enhanced after ultrafiltration.
出处
《林产化学与工业》
EI
CAS
CSCD
北大核心
2011年第5期37-40,共4页
Chemistry and Industry of Forest Products
基金
江苏大学博士研究生科研创新计划(CX10B_007X)
江苏高校优势学科建设工程资助项目(无编号)
关键词
水飞蓟蛋白
酶解
超滤
抗氧化活性
Silybum marianum protein
enzymatic hydrolysis
ultrafiltration
antioxidant activity
