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Optimal conditions of enzymatic hydrolysis for producing anti-inflammatory peptides from sandfish (Arctoscopus japonicus) hydrolysate

도루묵 가수분해물 유래 항염증 펩타이드 제조를 위한 효소 가수분해 최적 조건

  • 장혜림 (영남대학교 식품영양학과) ;
  • 윤경영 (영남대학교 식품영양학과)
  • Received : 2017.08.14
  • Accepted : 2017.10.06
  • Published : 2018.04.30

Abstract

In this study, the hydrolysis conditions for the production of anti-inflammatory peptides from meat and roe hydrolysates of sandfish (Arctoscopus japonicus) were determined by measuring the nitric oxide (NO) scavenging enzymatic activity, experimental pH, temperature, enzyme concentration, and hydrolysis time. The optimal conditions determined when using meat hydrolysate were a pH value of 5.0, at a temperature of $30^{\circ}C$, 1% enzyme concentration, and 4 h hydrolysis time. The optimal conditions when using roe hydrolysate were a pH of 5.0, a temperature of $70^{\circ}C$, enzyme concentration of 3%, and hydrolysis time of 3 h. The NO scavenging activities of meat and roe hydrolysate were determined to be 18.94 and 19.81%, respectively. In summary, this study determined the optimum enzymatic hydrolysis conditions for the production of anti-inflammatory peptides from sandfish.

Keywords

sandfish;Arctoscopus japonicus;enzymatic hydrolysis;hydrolysis conditions;anti-inflammatory peptide

References

  1. Ahn CB, Je JY, Cho YS. Antioxidant and anti-inflammatory peptide fraction from salmon byproduct protein hydrolysates by peptic hydrolysis. Food Res. Int. 49: 92-98 (2012) https://doi.org/10.1016/j.foodres.2012.08.002
  2. An HC, Lee KH, Lee SI, Park HH, Bae BS, Yang JH, Kim JB. Behaviour habitats of sailfin sandfish, Arctoscopus japonicus approaching toward the eastern coastal waters of Korea in the spawning season. Jour. Fish. Mar. Sci. Edu. 23: 35-42 (2011)
  3. Bell LN. Peptide stability in solids and solutions. Biotechnol. Progr. 13: 342-346 (1997) https://doi.org/10.1021/bp970057y
  4. Bell LN, Labuza TP. Aspartame degradation kinetics as affected by pH in intermediate and low moisture food systems. J. Food Sci. 56: 17-20 (1991) https://doi.org/10.1111/j.1365-2621.1991.tb07964.x
  5. Bogdan C. Nitric oxide and the immune response. Nat. Immunol. 2: 907-916 (2001) https://doi.org/10.1038/ni1001-907
  6. Choi KH, Nam HH, Choo BK. Effect of five Korean native Taraxacum on antioxidant activity and nitric oxide production inhibitory activity. Korean J. Medicinal Crop Sci. 21: 191-196 (2013) https://doi.org/10.7783/KJMCS.2013.21.3.191
  7. Cordova-Murueta JH, Garcia-Carreno FL. Nutritive value of squid and hydrolyzed protein supplement in shrimp feed. Aquaculture 210: 371-384 (2002) https://doi.org/10.1016/S0044-8486(02)00011-X
  8. De Mejia EG, Dia VP. Lunasin and lunasin-like peptides inhibit inflammation through suppression of NF-${\kappa}B$ pathway in the macrophage. Peptides 30: 2388-2398 (2009) https://doi.org/10.1016/j.peptides.2009.08.005
  9. Dia VP, Wang W, Oh VL, De Lumen BO, De Mejia EG. Isolation, purification and characterisation of lunasin from defatted soybean flour and in vitro evaluation of its anti-inflammatory activity. Food Chem. 114: 108-115 (2009) https://doi.org/10.1016/j.foodchem.2008.09.023
  10. Griess P. Bemerkungen zu der Abhandlung der HH. Weselsky und Benedikt "Ueber einige Azoverbindungen". Ber. Deutsch. Chem. Ges. 12: 426-428 (1879) https://doi.org/10.1002/cber.187901201117
  11. Hernandez-Ledesma B, Hsieh CC, Ben O. Antioxidant and antiinflammatory properties of cancer preventive peptide lunasin in RAW 264.7 macrophages. Biochem. Bioph. Res. Co. 390: 803- 808 (2009) https://doi.org/10.1016/j.bbrc.2009.10.053
  12. Jang HL, Liceaga AM, Yoon KY. Purification, characterisation and stability of an antioxidant peptide derived from sandfish (Arctoscopus japonicus) protein hydrolysates. J. Funct. Foods 20: 433-442 (2016) https://doi.org/10.1016/j.jff.2015.11.020
  13. Jang HL, Liceaga AM, Yoon KY. Isolation and characteristics of anti-inflammatory peptides from enzymatic hydrolysates of sandfish (Arctoscopus japonicus) protein. J. Aquat. Food Prod. T. 26: 234-244 (2017a) https://doi.org/10.1080/10498850.2016.1221015
  14. Jang HL, Shin SR, Yoon KY. Hydrolysis conditions for antioxidant peptides derived from enzymatic hydrolysates of sandfish (Arctoscopus japonicus). Food Sci. Biotechnol. 26: 1191-1197 (2017b) https://doi.org/10.1007/s10068-017-0178-z
  15. Jun JY, Lim YS, Lee MH, Kim BM, Jeong IH. Changes in the physiochemical quality of sailfin sandfish Arctoscopus japonicus sauces fermented with soybean koji or rice koji during storage at room temperature. Korean J. Fish. Aquat. Sci. 49: 101-108 (2016)
  16. Lardner A. The effects of extracellular pH on immune function. J. Leukocyte Biol. 69: 522-530 (2001)
  17. Liu B, Gao HM, Wang JY, Jeohn GH, Cooper CL, Hong JS. Role of nitric oxide in inflammationmediated neurodegeneration. Ann. NY Acad. Sci. 962: 318-331 (2002) https://doi.org/10.1111/j.1749-6632.2002.tb04077.x
  18. Menard R, Khouri HE, Plouffe C, Dupras R, Ripoll D, Vernet T, Tessier DC, Laliberte F, Thomas DY, Storer AC. A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain. Biochemistry 29: 6706-6713 (1990) https://doi.org/10.1021/bi00480a021
  19. Nam HJ, Oh AR, Nam ST, Kang JK, Chang JS, Kim DH, Lee JH, Hwang JS, Shong KE, Park MJ, Seok H, Kim H. The insect peptide CopA3 inhibits lipopolysaccharideinduced macrophage activation. J. Pept. Sci. 18: 650-656 (2012) https://doi.org/10.1002/psc.2437
  20. Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87: 315-424 (2007) https://doi.org/10.1152/physrev.00029.2006
  21. Salvemini D, Misko TP, Masferrer JL, Seibert K, Currie MG, Needleman P. Nitric oxide activates cyclooxygenase enzymes. P. Natl. Acad. Sci. 90: 7240-7244 (1993) https://doi.org/10.1073/pnas.90.15.7240
  22. Schmidl MK, Taylor SL, Nordlee JA. Use of hydrolysate-based products in special medical diets. Food Technol. 48: 77-85 (1994)
  23. Senphan T, Benjakul S. Comparative study on virgin coconut oil extraction using protease from hepatopancreas of Pacific white shrimp and Alcalase. J. Food Process. Pres. 41: 1-12 (2016)
  24. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujinoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150: 76-85 (1985) https://doi.org/10.1016/0003-2697(85)90442-7
  25. Souissi N, Bougatef A, Triki-Ellouz Y, Nasri M. Biochemical and functional properties of sardinella (Sardinella aurita) by-product hydrolysates. Food Technol. Biotech. 45: 187-194 (2007)
  26. Southan GJ, Szabo C. Selective pharmacological inhibition of distinct nitric oxide synthase isoforms. Biochem. Pharmacol. 51: 383-394 (1996) https://doi.org/10.1016/0006-2952(95)02099-3
  27. Udenigwe CC, Lu YL, Han CH, Hou WC, Aluko RE. Flaxseed protein- derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages. Food Chem. 116: 277-284 (2009) https://doi.org/10.1016/j.foodchem.2009.02.046
  28. Yust M, Pedroche J, Giron-Calle J, Alaiz M, Millan F, Vioque J. Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase. Food Chem. 81: 363-369 (2003) https://doi.org/10.1016/S0308-8146(02)00431-4
  29. Zhuang Y, Sun L. Preparation of reactive oxygen scavenging peptides from tilapia (Oreochromis niloticus) skin gelatin: Optimization using response surface methodology. J. Food Sci. 76: C483- C489 (2011) https://doi.org/10.1111/j.1750-3841.2011.02108.x