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采用复合蛋白酶水解低次烟叶蛋白,产生的酶解物中蛋白肽根据其分子量大小进行了分离,在此基础上采用氧化亚油酸体系TBA法和DPPH自由基清除活性研究了不同肽组分的抗氧化活性。低次烟叶蛋白酶解液经超滤膜分级分离,得到透过10 kDa、5 kDa、3 kDa和1kDa 4种截留分子量膜的肽组分,其中透过5 kDa的肽组分具有较高的抗氧化活性,其氧化抑制率为42 .55 %,是原蛋白酶解液活性的2倍左右,接近VE的抗氧化活性。透过5 kDa的肽组分对DPPH自由基的清除活性最强(清除率达到83 .82 %) ,略低于VE的清除活性。试验结果表明,低次烟叶蛋白经复合蛋白酶酶解后产生的蛋白肽功能特性有明显的改善。
The composite proteinase was used to hydrolyze low-order tobacco leaf protein, and the protein peptide of the hydrolyzate was separated according to its molecular weight. On this basis, the oxidative linoleic acid system TBA method and DPPH radical scavenging activity were used to study the effects of different peptide components Antioxidant activity. Low-grade tobacco leaf proteolysis solution was fractionated by ultrafiltration to obtain peptide components that permeated through 4 molecular weight cut-offs of 10 kDa, 5 kDa, 3 kDa and 1 kDa, and the peptide component permeating 5 kDa had higher antifungal activity Oxidation activity, the oxidation inhibition rate of 42.55%, is the original proteolytic fluid activity of about 2 times, close to the VE antioxidant activity. The DPPH radical scavenging activity through the 5 kDa peptide component was strongest (83.82% clearance), slightly lower than the scavenging activity of VE. The experimental results showed that the functional properties of the protein peptide produced by the low protease of the low-grade tobacco leaf protein were significantly improved.