Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria
Stanisavljević, Nemanja S. (Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia)) | Vukotić, Goran N. (Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia)) | Pastor, Ferenc T. (Faculty of Chemistry, Belgrade (Serbia)) | Sužnjević, Desanka (Institute of General and Physical Chemistry, Belgrade (Serbia)) | Jovanović, Živko S. (Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia)) | Strahinić, Ivana D. (Institute of Molecular Genetics and Genetic Engineering, Belgrade (Serbia)) | Fira, Đorđe A. (Faculty of Biology, Belgrade (Serbia)) | Radović, Svetlana S. (Faculty of Biology, Belgrade (Serbia))
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, Fe3+-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.
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