Edamame protein hydrolysis using Lactococcus lactis, Lactobacillus bulgaricus and Lactobacillus paracasei produce short peptides with higher antioxidant potential

Abstract

Abstract. Anggraeni SL, Jayus J, Ratnadewi AAI, Nurhayati N. 2022. Edamame protein hydrolysis using Lactococcus lactis, Lactobacillus bulgaricus and Lactobacillus paracasei produce short peptides with higher antioxidant potential. Biodiversitas 23: 3604-3613. The high demand for protein sources for functional vegetable foods, especially proteins that have ACE (Angiotensin-Converting Enzyme) inhibitory activity has encouraged efforts to meet this need through exploration of potential protein sources and the development of food processing technology to modify the protein into derivative compounds in the form of short peptides to promote higher bioactivity than the native protein. This research focused on the hydrolysis of edamame proteins into shorter peptides through a fermentation process using a group of Lactic Acid Bacteria (LABs), that is Lactococcus lactis, Lactobacillus bulgaricus and L. paracasei, to gain a higher functional activity of its protein hydrolysate. Edamame milk was fermented with that LABs as starter culture until 24 hours at 37ºC. The activity of the protease released by the LABs was confirmed using the agar diffusion method based on the emergence of a clear zone surrounding the culture, while the antioxidant activity was confirmed with the ABTS and hydroxyl radical scavenging methods. The results exhibited that the population density of starter culture in edamame milk reached 108 CFU/mL, and the pH decreased from 6.75 to 4.15. All LABs used in fermentation were able to hydrolyze protein as indicated by the increasing degree of hydrolysis and changes in protein profile of SDS-PAGE analysis. In addition, when compared to the unfermented edamame milk, the protein hydrolysate from LABs fermentation showed an increase of ABTS and hydroxyl radical inhibitory activity, in which the highest IC50 values ??of 8.96 and 13.33 g/mL of each were found in edamame milk fermented by Lc. lactis InaCC B187. An increase in ACE inhibitory activity was also observed in edamame milk fermented using this microbe (9.80 g/µL). These findings indicate that Lc. lactis InaCC B187, L. delbrueckii subspecies bulgaricus FNCC41, and L. paracasei InaCC B145 have the potency as an effective starter culture to increase bioactive peptides in edamame soybeans potential for functional food sources.

Fermentation of Peanut Slurry with Lactococcus lactis Species, Leuconostoc and Propionibacterium freudenreichii subsp. globosum Enhanced Protein Digestibility

“…Lactococcus lactis are proteolytic microbes that produce proteases during cell growth [ 25 , 26 ]. In a previous study, Lactococcus lactis was used as a proteolytic microbe to obtain bioactive peptides from soymilk through fermentation [ 27 ]. After fermentation, the soymilk had 2875 U/mL of protease activity, and the degree of hydrolysis value reached 44.32%.…”

“…After fermentation, the soymilk had 2875 U/mL of protease activity, and the degree of hydrolysis value reached 44.32%. The degree of hydrolysis was assessed with the trinitro-benzene-sulfonic acid assay and calculated as the ratio between the increase in amino acid content after hydrolysis and the total peptide content, with the result expressed as a percentage [ 27 ]. Leuconostoc may also have a proteolytic ability.…”

Identification of lactic acid bacteria isolated from developed dried coffee starter culture used as a fermentation agent to produce Robusta civet coffee

“…A selected lactic acid bacterium, Lactobacillus plantarum LPBR01 was able accelerate coffee-pulp acidification process (Pereira et al 2016), since this bacterium is able to produce several lactic acids as their metabolite (De Carvalho Neto et al 2018). This bacterium strain may also able to produce some glycolytic (Lovabyta et al 2020) and proteolytic enzymes (Anggraeni et al 2022) during fermentation, which may be able to degrade complex carbohydrate and protein presence in the coffee mucilage layer (Febrianto and Zhu 2023).…”

The recombinant expression and antimicrobial activity determination of Cecropin-like part of Heteroscorpine-1 from Heterometrus laoticus

“…The expressed peptide was analyzed by SDS-PAGE system containing 4% of polyacrylamide gel as a stacking gel and 13% of polyacrylamide gel as a separating gel (Anggraeni et al 2022). The peptide was mixed with 0.5 mM Tris-HCl pH 6.8, 0.5% (w/v) bromophenol blue, 10% (v/v) glycerol, 2% (w/v) SDS, and 10% (v/v) βmercaptoethanol, heated in boiling water for 5 min, and loaded to the gel 15 μL.…”