Table 2.
Q-values of peptides produced during the hydrolysis of various proteins using different hydrolysis conditions.
| Protein source | Identified peptide sequences (Q value)a | Hydrolysis conditionsb | Bitterness evaluation method | Factors influencing bitterness | Bioactivities | References |
|---|---|---|---|---|---|---|
| Milk | VLPVPQK (1876), EIVESLSSSEESITRINK (972), FLLY (2189), PFPIIV (2810), SDISLLDA (1171), TTMPL (1324), ESISSSEEIV (983), FPQY (2088), PPFL (2707), IESPPEIN (1660), DERFFSDK (1233), MMSFV (1591), PTPEG (1272), TTMPLW (1739), MPFPK (2383), VLSR (1185), SDISLLDA (1171), LLFCME (1814), NLPPLTA (1551), SFLY (1918), LCVLH (1683), KHQGL (890), KEGI (1341), KKNQDKTEI (1001), DAQSAP (825) | Bromelain (50 °C, pH = 7), proteinase K (37 °C, pH = 7), papain (65 °C, pH = 7), and ficin (50 °C, pH = 6.5); E/S: 1/100 (w/w); time: 3 h | BIOPEP-UWM database prediction | Hydrophobicity and enzyme active site | Antioxidative, opioid, immunomodulating, ACE inhibitory | 200 |
| LLYQEPVLGPVRGPFPIIV (1933), LYQEPVLGPVRGPFPI (1848), LYQEPVLGPVRGPFP (1760), LYQEPVLGPVRGPFPIIV (1921), LLYQEPVLGPVRGPFP (1784), FFVAPFPEVFGK (2000) | Flavourzyme (50–55 °C, pH = 5.5–7.5), protamex (50 °C, pH = 7–8), promod 523MDPTM (45–55 °C, pH = 5–7), and flavorpro 937MDPTM (50 °C, pH = 5–7); time: 9 h | Taste panelists | Degree of hydrolysis | – | 201 | |
| – | Trypsin (40 °C); E/S: 0.008–0.032 g/L; time: 10 min | Taste panelists | Hydrophobicity | – | 35 | |
| VEELKPTPEGDLEIL (1452), VEE (1009), LKPTPE (1685), GDLE (831), IL (2660) | Alcalase 2.4 L, prolyve 1000 and corolase 7089; 50 °C; pH = 7, E/S: 0.25% | Taste panelists | Hydrophobicity | – | 47 | |
| VLVLDTDYK (1487), GLDIQK (1234), IDALNEK (1269), TPEVDDEALEK (1109), VGINYWLAHK (1684), HIRLS (1374), KTKIPAVF (1845), MAASDISLL (1247), VRTPEVDDE (1075), LVRTPEVDDE (1183), VRTPEVDDEALE (1102), LVRTPEVDDEALE (1182), VLPVPQ (1922), KAVPYPQ (1802), RDMPIQAF (1580), SQSKVLPVPQ (1297), PEGDLEI (1426), VEELKPT (1378), VEELKPTPE (1460), AVPYPQ (1835) | Alcalase (65 °C, pH = 8.5, E/S: 1/100, time: 5 h), corolase PP (45 °C, pH = 7.5, E/S: 1/50, time: 7 h), flavourzyme (50 °C, pH = 6.5, E/s: 1/100, time: 8 h) | Taste panelists | Enzyme active site | Antioxidative | 202 | |
| – | Alcalase (55 °C, pH = 8.5), protamex (50 °C, pH = 6.5), flavourzyme (50 °C, pH = 7); E/S: 1/50; time: 30–180 min | E-tongue measurement | Enzyme active site | – | 26 | |
| – | Commercial protein hydrolysates | Taste panelists | Degree of hydrolysis and hydrophobicity | – | 43,203 | |
| Soybean | FLS (1666), LLPH (2000), INGY (1458), IYIG (2253), VYDV (1734), SVIY (1913), VYFV (2309), ISIY (2245), VVLY (2126), DIF (2211), GYPVV (1851), YVVL (2126), SGFTL (993), SNLNFL (1188) | Alcalase (50 °C, pH = 8, E/S: 12 AU/Kg) | Taste panelists | Hydrophobicity | – | 204 |
| LSVISPK (1657), DVLVIPLG (1829), LIVILNG (1781), NPFLFG (1800), ISSTIV (1348), PQMIIV (2102), PFPSIL (2328), DDFFL (1815), FFEITPEK (1823) |
Bromelain (50 °C, pH = 7), proteinase K (37 °C, pH = 7), papain (65 °C, pH = 7), and ficin (50 °C, pH =6.5); E/S: 1/100 (w/w); time: 3 h |
BIOPEP-UWM database prediction | Hydrophobicity and enzyme active site | Antioxidative, opioid, immunomodulating, ACE inhibitory | 205 | |
| AFPGSAKDIENLIK (1443), YVVNPDNNENLRLITL (1297), RRPSYTNGPQEIY (1253), SLENQLDQMPRRF (1092), VVNPDNNENLRLITL (1205), RIDPELEKEIGAK (1425), ENQLDQMPRRF (1099), SLLNALPEEVIQHTFNLK (1311), NQLDQMPRRF (1149), RAELSEQDIFVIPA (1437), LVPPQESQRR (1171), IIDTNSLENQLDQMPRRFYLA (1271), GINAENNQRNFLA (848), KLHENIARPS (1275), IVRNLQGENEEEDSGAIVTVK (950), LSIVDMNEGALLLPHFNSK (1332), AGANSLLNALPEEVIQH (1094), RVSDDEFNNY (988), NALEPDHRVESE (966), LAGNPDIEHPETM (1237), GKHQQEEENEGGSIL (656), EQGGEQGLEYVVF (997) | Protex 6 L (55 °C, pH = 8), protease A 2 SD (50 °C, pH = 7); E/S: 0.5%; time: 1–5 h | Taste panelists | Hydrophobicity and enzyme active site | Antioxidative | 24 | |
| Corn | – | Flavourzyme (50 °C, pH = 7), alcalase (50 °C, pH = 8), neutrase (50 °C, pH = 7), papain (55 °C, Ph = 7), and trypsin (40 °C, pH = 7.5); E/S: 3%; time: 10–100 min | Taste panelists | Degree of hydrolysis and hydrophobicity | ACE inhibitory | 65 |
| Fish | KAEPAPAPAPAPAPAPAPAP (1775), DEKSPAMPVPGPM (1558), GPAGPRGPSGERGEVGPA (986), LDKNKDPLNDSVVQ (1120), FAGDDAPRA (1125), SGPPVPGPIGPM (1759), LGAGDTDGDGKIGAD (721), DEKSPAMPVPGPMGPM (1549), IEDPFDQDDWEH (1415), LEQQVDDLEGSLE (846), APDPGPGPMG (1461), NWDDMEKIW (1754), GPPVPGPIGPM (1922), ERLEDEEEIN (963), AVIDQDKSGFIEEDELKLF (1349), RDLTDYLMK (1346), MPVPGPMGPM (1834), GPPVPGPIGPMG (1762), LGEQIDNLQRVK (1054), DPFDQDDWEHWAK (1495), GVDNPGHPF (1321), EDDIHPRNPPKFD (1558), MDEPVVVPGKPY (1775), GWLDKNKDPLNDSVVQ (1218), FIEEDELKLF (1719), SVDDEFPDLTK (1241), AGDDAPRAVFPS (1236), DRPGPPDGPLE (1480), SPAMPVPGPM (1747), GPSGKDGPRGPRGD (928), GEEGKRGPTGEIG (784), LDLPGPPIGPIN (1901), DLPGPPIGPIN (1878), GPAGPRGPSGA (1004), PPVPGPIGPM (2114), DRPGPPDGPLEVK (1517) | Neutrase (50 °C, pH = 7, E/S: 0.4–0.8%), bromelain (50 °C, pH = 7, E/S: 0.6–0.8%), flavourzyme (50 °C, pH = 7, E/S: 0.8%), protamex (50 °C, pH =7, E/S: 0.4–0.6%), papain (55 °C, pH = 7, E/S: 0.6–0.8%), and alcalase (55 °C, pH = 9, E/S: 0.6–0.8%); time: 2–10 h | Taste panelists | Hydrophobicity and enzyme active site | – | 25 |
| – | FoodPro PNL enzyme, 55 °C, E/S: 0.17–0.22 w/w, time: 50 min | Taste panelists | Hydrophobicity and enzyme active site | – | 206 | |
| – | Papain (pH = 7), trypsin (pH = 8), pepsin (pH = 2), alkaline (pH = 10) and flavourzyme (pH = 6); 50 °C; E/S: 100 U/g; time: 150 min | Taste panelists | Enzyme active site | Leucocytes and lysozyme activity | 207 | |
| – | Protamex (40 °C, pH = 6), alcalase (60 °C, pH = 8), trypsin (38 °C, pH = 8), flavourzyme (50 °C, pH = 6) and neutrase (45 °C, pH = 7); E/S: 2%; time: 5 h | Taste panelists | Hydrophobicity and enzyme active site | – | 208 | |
| Seaweed | – | Protease A ‘Amano’ G (50 °C, pH = 7), protease M ‘Amano’ (50 °C, pH = 4.5), protease N ‘Amano’ (55 °C, pH = 7), protease P ‘Amano’ 3G (45 °C, pH = 8), protease S ‘Amano’ (70 °C, pH = 8), blomelain F (60 °C, pH = 9), proleather FG-F (60 °C, pH = 10), peptidase R (45 °C, pH = 7), umamizyme (50 °C, pH = 7), newlase F (45 °C, pH = 3), papain W-40 (65 °C, pH = 7), pancreatine F (45 °C, pH = 9), pepsin (45 °C, pH = 2), denazyme AP (50 °C, pH = 7), denapsin 10P (50 °C, pH = 3), XP-415 (55 °C, pH = 3), alcalase 2.4 L FG (60 °C, pH = 7), E/S: 1%; time: 18 h | – | Hydrophobicity | ACE inhibitory | 209 |
| Synthetic peptides | YGLF (1926), YPFPGPIPN (2257), IPAVF (2318), LLF (2393) | – | Taste panelists | Hydrophobicity | – | 121 |
| MPFPKYPVEPF (2336), GPVRGPFPIIV (2034), MAPKHKEMPFPKYPVEPF (1979), APHGKEMPFPKYPVEPF (1905) | – | Taste panelists | Hydrophobicity | – | 210 | |
| Bovine muscle | – | Alcalase (50 °C, pH = 7.5), flavourzyme (50 °C, pH = 7), protamex (55 °C, pH = 7.5), neutrase (50 °C, pH = 7), proteAX (50 °C, pH = 7), protease P 6 SD (40 °C, pH = 7), protease A 2 SD (50 °C, pH = 7), papain P1 (55 °C, pH = 7), bromelain (40 °C, pH = 7) and sumizyme BNP-L (50 °C, pH = 7); E/S: 0.5%; time: 1–5 h | Taste panelists | Degree of hydrolysis and enzyme active site | – | 150 |
| Porcine plasma | – | Taste panelists | ||||
| Bovine hemoglobin | VVYPWTQR (1715), VVYPW (2614) | Pepsin (37 °C, pH = 3) | Taste panelists | Hydrophobicity | – | 211 |
| Pea | – | Alcalase (50 °C, pH = 8), flavourzyme (50 °C, pH = 7), papain (40 °C, pH = 6.5), trypsin and α-chymotrypsin (37 °C, pH = 8); E/S: 4%; time: 4 h | Taste panelists | Hydrophobicity and enzyme active site | Antioxidative, ACE inhibitory | 84 |
| – | Alcalase (55 °C, pH = 8.5, E/S: 3%, time: 2.5 h) followed by protemax (50 °C, pH = 7, E/S: 1%, time: 1 h) | Taste panelists | Hydrophobicity | ACE and DPP-IV inhibitory | 87 | |
| Peanut | – | Multifect PR 6 L and flavorzyme (pH = 9.5), protamex, neutrase, and Papain (pH = 7.5); 45 °C | E-tongue measurement | Degree of hydrolysis | – | 212 |
| Soy, pea, and canola | – | Flavourzyme 1000 L, protease P “Amano” 6 SD, deltazymAPS-M-FG, promod278, proteAX-K, and peptidase R; pH = 7.3; 50 °C; E/S: 2%; time: 2 h | Taste panelists | Hydrophobicity and enzyme active site | – | 213 |
| Chickpea | LR (1465), PLLVE (1926), SPKAGAGK (959), HATGGGSGR (257), PHPATSGGGL (949), TPKASATAAL (976), TLTTGTGGLL (632), YVDGSGTPLT (1005), TKTPGAGTSAGL (677), KEGGGTGTGAAR (376), STGPNAGGGAGGY (546), TLLFTELLF (1654), KNGAAGPSTVAR (787), LASEGASAATGAF (733), VLTSGAGSGAAALT (658), KNGLGAGAGAGSAR (549), LSAHAGGTGATLW (863), LDLARAGGCPTKN (1015), SPQSPPFATPLW (1754), LLSASMGSQLLSF (1053), GKGSGAF (750), TRGTGGR (214), KMTAGSGVT (642), KSGGGGGGTAVT (345), GKAAPGSGGGTKA (649), RASAAGGGGGGVSSR (380), GKGSSGTGAGGASVSGVT (372), NKKSGAGGGSGAGKGGVA (498), LLGELCGSGNTVVEL (991), QNPLSSAAPTGAGKPY (1082), GLTQGASLAGSGAPSPLF (961), AMMELGWSTSGEFLL (1220) | Pepsin/pancreatin (E/S: 1/50), bromelain (55 °C, pH = 5.5–6.5, E/S: 1/50, time: 30 min) | BIOPEP database prediction | Hydrophobicity | DPP-IV, DPP-III, ACE, renin, α-glucosidae and α-amylase inhibitory, Antiamnestic, antithrombotic, antioxidative, hypolipidemic, HMG-CoA reductase | 214 |
| Flaxseed | – | Alcalase (3000 U/g, 60 °C, pH = 8), flavourzyme (120 U/g, 50 °C, pH = 6.5); time: 2 h | Taste panelists | Degree of hydrolysis, hydrophobicity, and enzyme active site | – | 215 |
| Cricket and mealworm | – | Flavourzyme 1000 L, protease P “Amano” 6 SD; pH = 7.3; 50 °C; E/S: 2%; time: 2 h | Taste panelists | Enzyme active site | – | 216 |
aValues in brackets are Q values calculated following the formula as described in Eq. 1.
bAbbreviation E/S indicates the ratio of enzyme to substrate.