DOI QR코드

DOI QR Code

Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas

살 오징어(Todarodes pacificus) 간췌장으로부터 aminopeptidase 활성 획분의 쓴맛 개선 효과

  • Received : 2014.07.23
  • Accepted : 2014.10.14
  • Published : 2014.12.31

Abstract

Aminopeptidase-active fractions from crude extract of the hepatopancreas of a common squid (Todarodes pacificus) were obtained using acetone (AC; 30-40%) and ammonium sulfate precipitation (AS; 60-70% saturation), anion exchange (AE-II; 0.2 M NaCl) and gel filtration chromatography (GF-I; 30-50 kDa), respectively. The debittering capacity of GF-I fraction based on the aminopeptidase activity (89.2 U/mg), recovery (56.6%) and sensory evaluation (1.0) was better than that of other fractions. Release of amino acids increased as incubation time was increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides, as revealed by reverse-phase HPLC profiles. Peaks 3, 5 and 6 showed the decreased area (%), whereas peaks 1, 2 and 4 showed the increased area. The GF-I fractions were found to be suitable for reducing bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides.

Keywords

common squid;hepatopancreas;aminopeptidase;debittering;fractionation

References

  1. Okutani T. Cuttlefishes and Squid of the World. Seizando, Tokyo, Japan. p. 198 (2005)
  2. Stansby ME. 1976. Fish Oils in Nutrition. New York, NY, USA. pp. 6-39 (1976)
  3. Ministry of Oceans and Fisheries. Year book of marine resources. Available from: http://stat.mof.go.kr/portal/bbs/selectBbsArticle.do?bbsId=BBSMSTR_000000000006&nttId=62. Accessed Apr. 14, 2013.
  4. Gildberg A. Purification and characterization of cathepsin D from the digestive gland of the pelagic squid Todarodes sagittatus. J. Sci. Food Agr. 39: 85-94 (1987) https://doi.org/10.1002/jsfa.2740390110
  5. Raksakulthai R, Harrd NF. Purification and characterization of a carboxypeptidase from squid hepatopancreas (Illex illecebrosus). J. Agr. Food Chem. 49: 5019-5030 (2001) https://doi.org/10.1021/jf010320h
  6. Raksakulthai R, Harrd NF. Purification and characterization of aminopeptidase fractions from squid (Illex illecebrosus) hepatopancreas. J. Food Biochem. 23: 123-144 (1999) https://doi.org/10.1111/j.1745-4514.1999.tb00010.x
  7. Hameed KS, Haard NF. Isolation and characterization of cathepsin C from atlantic short finned squid Illex illecebrosus. Comp. Biochem. Physiol. 82B: 241 - 246 (1985)
  8. Heu MS, Ahn SH. Development and fractionation of proteolytic enzymes from an inedible seafood product. J. Korean Fish. Soc. 32: 458-465 (1999)
  9. Kim HS, Heu MS, Kim JS. Distribution and extraction condition of endoprotease and exoprotease from viscera of Illex argentinus. J. Korean Soc. Appl. Biol. Chem. 50: 308-315 (2007)
  10. Kim MJ, Kim HJ, Kim KH, Heu MS, Kim JS. Endoprotease and exopeptidase activities in the hepatopancreas of the cuttlefish Sepia officinalis, the squid Todarodes pacificus, and the octopus Octopus vulgaris Cuvier. Fish. Aquat. Sci. 15: 197-202 (2012) https://doi.org/10.5657/FAS.2012.0197
  11. Kim HS, Kim JS, Heu MS. Fractionation of endoprotease from viscera of Argentina shortfin squid, Illex argentinus. J. Korean Fish. Soc. 41: 176-181 (2008) https://doi.org/10.5657/kfas.2008.41.3.176
  12. Kim HS, Kim JS, Heu MS. Fractionation of exopeptidase from viscera of Argentina shortfin Squid, Illex argentinus. J. Korean Soc. Food Sci. Nutr. 37: 1009-1017 (2008) https://doi.org/10.3746/jkfn.2008.37.8.1009
  13. Ishibashi N, Arita Y, Kanehisa H, Kogure K, Okai H, Fukui S. Bitterness of leucine-containing peptides. Agr. Biol. Chem. 59: 2389-2394 (1987)
  14. Kim MJ, Kim HJ, Kim KH, Heu MS, Lee JS, Kim JS. Fractionation and enzymatic characterization of endoprotease and exopeptidase from crude extracts of cuttlefish Sepia officinalis hepatopancreas. Fish. Aquat. Sci. 15: 283-291 (2012) https://doi.org/10.5657/FAS.2012.0283
  15. Haard NF. Protein hydrolysis in seafoods: In Seafoods Chemistry, Processing Technology and Quality. Shahidi F. Springer, New York, NY, USA, pp. 10-33 (1994)
  16. Liu F, Yasuda M. Debittering effect of Monascus carboxypeptidase during the hydrolysis of soybean protein. J. Indian Microbiol. Biotechnol. 32: 487-489 (2005) https://doi.org/10.1007/s10295-005-0024-9
  17. Kim JS, Kim MJ, Kim KH, Kang SI, Park SH, Lee HJ, Heu MS. Debittering of enzymatic hydrolysate using exopeptidase active fractions from the Argentina shortfin squid Illex argentinus hepatopancreas. J. Korean Fish. Soc. 49: 142-149 (2014)
  18. Capiralla H, Hiroi T, Horokawa T, Maeda S. Purification and characterization of hydrophobic amino acids-specific endopeptidase from Halobacterium halobium S9 with potential application in debittering of protein hydrolysates. Process Biochem. 38: 571-579 (2002) https://doi.org/10.1016/S0032-9592(02)00180-2
  19. Nishiwaki T, Yoshimizu S, Furuta M, Hayashi K. Debittering of enzymatic hydrolysates using an aminopeptidase from edible Basidiomycete Grifola frondosa. J. Biosci. Bioeng. 93: 60-63 (2002) https://doi.org/10.1016/S1389-1723(02)80055-X
  20. Saha BC, Hayashi K. Debittering of protein hydrolyzates. Biotech. Advances 19: 355-370 (2001) https://doi.org/10.1016/S0734-9750(01)00070-2
  21. Izawa N, Tokuyasu K, Hayashi, K. Debittering of protein hydrolysates using Aeromonas caviae aminopeptidase. J. Agr. Food Chem. 45: 543-545 (1997) https://doi.org/10.1021/jf960784t
  22. Umetsu H, Ichishima E. Debittering mechanism of bitter peptides from soybean protein by wheat carboxypeptidase. J. Jpn. Soc. Food Sci. Technol. 35: 440-447 (1988) https://doi.org/10.3136/nskkk1962.35.440
  23. Tan PS, Van Kessel, TA, Van de Veerdonk FL, Zuurendonk PF, Bruins AP, Konings WN. Degradation and debittering of a tryptic digest from ${\beta}$-casein by aminopeptidase N from Lactococcus lactis sub sp. cremoris WG2. Appl. Environ. Microbiol. 59: 1430-1436 (1993)
  24. Dawson RMC, Elliot DC, Elliot WH, Jones KM. Data for Biochemical Research. 3rd ed. Oxford Univ Press, Oxford, UK, pp. 417-441 (1986)
  25. Lowry OH, Watanabe NJ, Farr AL, Randall RJ. Protein measurement with the folin-phenol reagent. J. Biol. Chem. 193: 265-275 (1951)
  26. Bumberger E, Belitz HD. Bitter taste of enzymic hydrolysates of casein. Z. Lebensm. Unters. For. 197: 14-19 (1993) https://doi.org/10.1007/BF01202693
  27. Matoba T, Hayashi R, Hata T. Isolation of bitter peptides from trypsin hydrolysate of casein and their chemical structure. Agr. Biol. Chem. 34: 1235-1243 (1970) https://doi.org/10.1271/bbb1961.34.1235
  28. Matoba T, Hayashi R, Hata T. Bitter peptides from tryptic hydrolysate of casein. Agr. Biol. Chem. 34: 1245-1241 (1970)
  29. Raksakulthai R, Rosenberg M, Haard NF. 2002. Accelerated cheddar cheese ripening with an aminopeptidase fraction from squid hepatopancreas. J. Food Sci. 67: 923-928 (2002) https://doi.org/10.1111/j.1365-2621.2002.tb09429.x
  30. Lin SB, Nelles LP, Cordle CT, Thomas RL. Debittering casein hydrolysates with octadecyl-siloxane (C18) columns. J. Food. Sci. 62: 665-670 (1997) https://doi.org/10.1111/j.1365-2621.1997.tb15431.x
  31. Ishibashi N, Sadamori K, Yamamoto O, Kanehisa H, Kogure K, Kikuch E, Okai H and Fukui S. Bitterness of phenylalanine- and tyrosine-containing peptides. Agr. Biol. Chem. 51: 3309-3313 (1987) https://doi.org/10.1271/bbb1961.51.3309
  32. Park SY, Lee BH. Effects of Lactobacillus casei LLG on flavor of enzyme-modified cheese. 1. Degradation of hydrophobic peptides by aminopeptidase. Korean J. Food Sci. Ani. Resour. 16: 147-154 (1996)

Cited by

  1. Recovery of serine protease inhibitor from fish roes by polyethylene glycol precipitation vol.19, pp.1, 2016, https://doi.org/10.1186/s41240-016-0016-x

Acknowledgement

Supported by : 한국연구재단