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Comparison of statistically significant changes between treatment groups for peptides, proteins by peptide count and proteins by total peptide abundance. Column 2: Number of peptides significantly different (p < 0.05) in abundance in treatment groups. Column 3: Number of proteins significantly different (p < 0.05) in unique peptide count between treatment groups. Column 4: Number of proteins significantly different (p < 0.05) in peptide abundance between treatment groups. The raw milk group, RM; the kefir group, K; the heat-treated milk groups with opened vials during incubation, HMo, and with closed vials during incubation, HMc.

Table 1 Comparison of statistically significant changes between treatment groups for peptides, proteins by peptide count and proteins by total peptide abundance. Column 2: Number of peptides significantly different (p < 0.05) in abundance in treatment groups. Column 3: Number of proteins significantly different (p < 0.05) in unique peptide count between treatment groups. Column 4: Number of proteins significantly different (p < 0.05) in peptide abundance between treatment groups. The raw milk group, RM; the kefir group, K; the heat-treated milk groups with opened vials during incubation, HMo, and with closed vials during incubation, HMc.

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Fig. 1. Electrophoresis gel (15% polyacrylamide gel) of the proteins in the raw milk group (RM), the kefir group (K), and the heat-treated milk groups without kefir with opened vials during incubation (HMo) and closed vials during incubation (HMc). Lanes A, B, C, D and E are 5 commercial kefir products for comparison.
Fig. 1. Electrophoresis gel (15% polyacrylamide gel) of the proteins in the raw milk group (RM), the kefir group (K), and the heat-treated milk groups without kefir with opened vials during incubation (HMo) and closed vials during incubation (HMc). Lanes A, B, C, D and E are 5 commercial kefir products for comparison.
Fig. 2. (A) Venn diagram of peptide numbers that were the same and unique in each group (raw milk group, RM; kefir group, K; heat-treated milk groups with opened vial during incubation, HMo, and with closed vials during incubation, HMc). A peptide present in at least one of a triplicate’s samples was considered present. (B) Venn diagram ¢ protein numbers that released peptides in the K, RM, HMo and HMc groups. A protein present in at least one of a triplicate’s samples was considered present.
Fig. 2. (A) Venn diagram of peptide numbers that were the same and unique in each group (raw milk group, RM; kefir group, K; heat-treated milk groups with opened vial during incubation, HMo, and with closed vials during incubation, HMc). A peptide present in at least one of a triplicate’s samples was considered present. (B) Venn diagram ¢ protein numbers that released peptides in the K, RM, HMo and HMc groups. A protein present in at least one of a triplicate’s samples was considered present.
Fig. 3. Peptide abundance for each protein by treatment group (K, RM, HMo and HMc; see Fig. 1 for abbreviations). The letters (a, b, c) indicate whether the peptide abundances between the different groups were significantly different (p < 0.05) for each protein. Values are mean + SEM. as1-casein, CASA1; os2-casein, CASA2; B-casein, CASB; glycosylation-dependent cell adhesion molecule 1, GLCM1; polymeric immunoglobulin receptor, PIGR; fibroblast growth factor-binding protein 1, FGFP1; osteopontin, OSTP; perilipin-2, PLIN2; butyrophilin subfamily 1 member A1, BT1A1; lipoprotein lipase, LIPL; lactoperoxidase, PERL; «-casein, CASK; mucin-1, MUC1; mucin-15, MUC15; serum amyloid A protein, Q56J78; B-1,4-galactosyltransferase 1, B4GT1; B-lactoglobulin, LACB; parathyroid hormone, PTHR; lactoferrin, TRFL; and o-lactalbumin, LALBA.
Fig. 3. Peptide abundance for each protein by treatment group (K, RM, HMo and HMc; see Fig. 1 for abbreviations). The letters (a, b, c) indicate whether the peptide abundances between the different groups were significantly different (p < 0.05) for each protein. Values are mean + SEM. as1-casein, CASA1; os2-casein, CASA2; B-casein, CASB; glycosylation-dependent cell adhesion molecule 1, GLCM1; polymeric immunoglobulin receptor, PIGR; fibroblast growth factor-binding protein 1, FGFP1; osteopontin, OSTP; perilipin-2, PLIN2; butyrophilin subfamily 1 member A1, BT1A1; lipoprotein lipase, LIPL; lactoperoxidase, PERL; «-casein, CASK; mucin-1, MUC1; mucin-15, MUC15; serum amyloid A protein, Q56J78; B-1,4-galactosyltransferase 1, B4GT1; B-lactoglobulin, LACB; parathyroid hormone, PTHR; lactoferrin, TRFL; and o-lactalbumin, LALBA.
“ p values were calculated by one-way ANOVA. Differences were considered significant when p < 0.05
“ p values were calculated by one-way ANOVA. Differences were considered significant when p < 0.05
Fig. 4. Relative abundance of taxonomic assignments by species, as assigned by MG-RAST annotation of shotgun 16S rRNA sequencing. Numerous findings indicated that the kefir microorganisms hydrolyzed milk proteins and peptides. 1039 peptides from 23 pro- teins present in the control groups were absent from the K sam- ples. These peptides were likely either hydrolyzed further by extracellular kefir microorganism proteases or taken up by the kefir microorganisms. Some kefir microorganisms, including Lacto- bacillus identified in the kefir grains used in the present study, have extracellular proteolytic capabilities. Many lactic acid bacteria are auxotrophic for several amino acids—that is, they depend on exter- nal amino acids for growth (Kunji et al., 1996). Lactobacillus have extracellular cell envelope proteinases that hydrolyze proteins into protein fragments (oligopeptides and amino acids) (Pritchard & Coolbear, 1993). Lactic acid bacteria transporters carry di- and tripeptides and an Opp protein system transports larger peptides into cells (Doeven, Kok, & Poolman, 2005; Savijoki, Ingmer, & Varmanen, 2006) where proteases hydrolyze small peptides to amino acids (Kunji et al., 1996). The action of the extracellular pro- teinase and peptide transport systems in Lactobacillus can explain the disappearance of large peptides in the K samples that were pre- sent in the control groups. This point aligns with the finding that the K samples contained statistically fewer peptides than the con- trol samples. The K samples contained 609 peptides derived from 20 proteins that were not present in the control samples were likely the result of the Lactobacillus extracellular proteinases. The finding that ~1500 peptides differed in intensity between K and the control groups (58.9% increased, 37.4% decreased) demon- strated that kefir microorganisms hydrolyzed proteins to release more peptides, and either further hydrolyzed or absorbed peptides present in the milk. That 40-45 proteins that differed in peptide count and 45-49 proteins differed in peptide abundance between K and the control groups also indicated that kefir microorganisms hydrolyzed milk proteins. Many protein total peptide intensities and total peptide counts of proteins were altered significantly in
Fig. 4. Relative abundance of taxonomic assignments by species, as assigned by MG-RAST annotation of shotgun 16S rRNA sequencing. Numerous findings indicated that the kefir microorganisms hydrolyzed milk proteins and peptides. 1039 peptides from 23 pro- teins present in the control groups were absent from the K sam- ples. These peptides were likely either hydrolyzed further by extracellular kefir microorganism proteases or taken up by the kefir microorganisms. Some kefir microorganisms, including Lacto- bacillus identified in the kefir grains used in the present study, have extracellular proteolytic capabilities. Many lactic acid bacteria are auxotrophic for several amino acids—that is, they depend on exter- nal amino acids for growth (Kunji et al., 1996). Lactobacillus have extracellular cell envelope proteinases that hydrolyze proteins into protein fragments (oligopeptides and amino acids) (Pritchard & Coolbear, 1993). Lactic acid bacteria transporters carry di- and tripeptides and an Opp protein system transports larger peptides into cells (Doeven, Kok, & Poolman, 2005; Savijoki, Ingmer, & Varmanen, 2006) where proteases hydrolyze small peptides to amino acids (Kunji et al., 1996). The action of the extracellular pro- teinase and peptide transport systems in Lactobacillus can explain the disappearance of large peptides in the K samples that were pre- sent in the control groups. This point aligns with the finding that the K samples contained statistically fewer peptides than the con- trol samples. The K samples contained 609 peptides derived from 20 proteins that were not present in the control samples were likely the result of the Lactobacillus extracellular proteinases. The finding that ~1500 peptides differed in intensity between K and the control groups (58.9% increased, 37.4% decreased) demon- strated that kefir microorganisms hydrolyzed proteins to release more peptides, and either further hydrolyzed or absorbed peptides present in the milk. That 40-45 proteins that differed in peptide count and 45-49 proteins differed in peptide abundance between K and the control groups also indicated that kefir microorganisms hydrolyzed milk proteins. Many protein total peptide intensities and total peptide counts of proteins were altered significantly in
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Fermented MilksKappa CaseinBeta-CaseinProtein digestion
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