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首页> 外文期刊>Archives of Biological Sciences >ANTIOXIDANT ACTIVITY OF PEA PROTEIN HYDROLYSATES PRODUCED BY BATCH FERMENTATION WITH LACTIC ACID BACTERIA
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ANTIOXIDANT ACTIVITY OF PEA PROTEIN HYDROLYSATES PRODUCED BY BATCH FERMENTATION WITH LACTIC ACID BACTERIA

机译:乳酸菌分批发酵产生的豌豆蛋白水解液的抗氧化剂活性。

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摘要

Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW <10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe~(3+)-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
机译:从我们的收集物中选择了九种已知具有表面蛋白酶活性的乳酸杆菌菌株,并测试了它们在基于豌豆种子蛋白的培养基中生长以及水解纯化的豌豆蛋白以产生具有抗氧化(AO)活性的肽的能力。鼠李糖乳杆菌BGT10和玉米乳杆菌LMG17315这两种菌株对豌豆蛋白表现出很强的蛋白水解活性。通过标准的分光光度法(DPPH,ABTS,Fe〜(3+)还原能力)测试了用鼠李糖乳杆菌BGT10发酵纯化的豌豆蛋白得到的豌豆水解产物级分MW <10 kDa的AO活性。最近开发的直流(DC)极谱测定法。使用离子交换色谱法分离获得的水解产物的低分子量馏分,而洗脱的馏分的AO活性通过灵敏的DC极谱法测定,无需事先浓缩样品。结果显示,低丰度馏分中含有碱性肽的部分具有最高的抗氧化活性。根据获得的结果,可以得出结论,鼠李糖乳杆菌BGT10应作为从豆类蛋白质大规模生产生物活性肽的候选菌株进行进一步研究。

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