DOI QR코드

DOI QR Code

Process Optimization of Meat Protein Hydrolysate of Ogae Wings by Response Surface Methodology and Its Characteristics Analysis

표면반응분석을 이용한 오계 날개육 단백질 가수분해 최적 생산 공정 개발과 생산물의 특성 분석

  • Kim, A Yeon (Department of Food and Biotechnology, Joongbu University) ;
  • Yoo, Sun Kyun (Department of Food and Biotechnology, Joongbu University)
  • 김아연 (중부대학교 식품생명과학과) ;
  • 유선균 (중부대학교 식품생명과학과)
  • Received : 2016.06.09
  • Accepted : 2016.06.16
  • Published : 2016.06.30

Abstract

Protein hydrolysate that shows physiological function such as antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was performed to optimize the hydrolysis of the wing's meat of Yosan-Ogae by a commercial protease. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 1 to 3%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 3%(w/v), and degree of hydrolysis was 68 to 69% at above conditions. The molecular weight of hydrolysate was distributed to 500-1,200 Da and showed typical peptides. The amino acids of peptides showing presumably antioxidant activity such as histidine, proline, methionine, cystein, tyrosine, tryptophan, phenylalanine comprised about 43.07%. The glutamic acid was 13.6%. Therefore, we expect that those products are useful as functional food ingredients.

식물 및 동물성 유래 펩타이드 형태의 단백질 가수분해물은 항산화, 고혈압 완화, 면역조절, 진통완화 및 항균작용 등 생리활성이 있는 것으로 알려져 왔다. 본 연구는 연산 오계의 날개육 단백질로부터 bromelain 프로티아제를 이용하여 펩타이드 형태의 단백질 가수분해 최적공정을 수행하고 생성물의 특성을 분석하였다. 최적공정은 표면반응 분석법을 이용하여 수행을 하였고 공정의 범위는 반응온도 $40-60^{\circ}C$, 반응 pH 6-8, 효소의 농도 1-3%(w/v)이었다. 오계 날개육의 단백질 최적 효소가수분해 공정조건은 효소 반응온도 $48-50^{\circ}C$, 반응 pH 7.0-7.2, 효소의 양은 3%(w/v)에서 결정 되었다. 이때 단백질 가수분해 수율은 68-69%에 도달하였다. 생산된 대부분 가수분해물의 분자량들은 전형적인 펩타이드인 분자량 500-1,200 Da로 분포되었다. 생산된 펩타이드 중에 항산화 기능을 보여주는 소수성 아미노산들 histidine, proline, methionine, cystein, tyrosine, tryptophan, phenylalanine 들이 43.07%을 차지하였다. 또한 구성아미노산의 함량 glutamic acid가 전체 구성아미노산의 13.6%로 가장 많은 함량을 차지하여 건강 기능 식품소재로서 활용할 가치가 높을 것으로 기대를 한다.

Keywords

References

  1. H.S. Chae, C.N. Ahn, Y.M. Yoo, J.S. Ham, J.M. Lee, S.K. Yoon. The effects of the high pressure boiled extracts (HPBE) of the ogol chicken with herbs on the hormones, cytokine, specific antibody of serum in rat. Korean J. Food Sci. Ani, 24: 283-292, 2004.
  2. H.S. Chae, Y.M. Yoo, C.N. Ahn, B.Y. Cho, J.M. Park, J.M. Lee, Y.K. Kim, S.G. Yun, Y.I. Choi. Chemioal and sensory characteristics of boiled extracted from crossbred chicken as affected by the level of flavourzyme. K. J. Poultry science, 3: 11-16. 2003.
  3. H.S. Yoo, K.H. Chung, K.J. Lee, D.H. Kim, J.H. An. Effect of Gallus gallus var. domesticus (Yeonsan ogolgye) extracts on osteoblast differentiation and osteoclast formation. Microbiol. Biotechnol. Lett. 43: 322-329, 2015. https://doi.org/10.4014/mbl.1508.08006
  4. C.M. Cho, C.K. Park, M.Y. Lee, I.D. Lew. Physicochemical characteristics of silky fowl (Gallus domesticus var. silkies). Korean J. Food Sci. Ani. 26: 306-314, 2006.
  5. M. Darewicz, A. Iwaniak. Biologically active peptides derived from milk proteins. Medycyna Weterynaryjna-Veterinary Medicine-Science and Practice, 70: 348-354, 2014.
  6. U. Grienke, J. Silke, D. Tasdemir. Bioactive compounds from marine mussels and their effects on human health. Food Chemistry, 142: 48-60, 2014. https://doi.org/10.1016/j.foodchem.2013.07.027
  7. K. Arihara, M. Ohata. Bioactive compounds in meat F. Toldra (Ed.), Meat biotechnology, Springer Science Business Media, LLC, New York, 231-249, 2008.
  8. B. Cigic, M. Zelenik-Blatnik. Preparation and characterization of chicken egg white hydrolysate. Acta Chimica Slovenica, 51: 177-188, 2004.
  9. E. Salminen, J. Rintala. Anaerobic digestion of organic solid poultry slaughterhouse waste a review. Bioresour. Technol., 83: 13-26, 2002. https://doi.org/10.1016/S0960-8524(01)00199-7
  10. E. Haque, R. Chand, S. Kapila. Biofunctional properties of vioactive peptides of nilk origin. Food Reviews International 25: 28-43, 2009.
  11. J.H. Baek, E.J, Jeong, S.Y. Jeon, Y.J. Cha. Taste components of the hydrolysate of snow crab chionoecetes japonicus cooker effluent as precursors of crab flavorings. Kor J Fish Aquat Sci., 45: 232-237, 2012.
  12. X. Fang, N. Xie, X. Chen, H. Yu, J. Chen. Optimization of antioxidant hydrolysate production from flying squid muscle protein using response surface methodology. Original Research Article Food and Bioproducts Processing. 90(4): 676-682, 2012. https://doi.org/10.1016/j.fbp.2012.04.001
  13. H.W. Seo, E.Y. Jung, G.W. Go, G.D. Kim, S.T. Joo, H.S. Yang. Optimization of ydrolysis conditions for bovine plasma protein using response surface methodology. Original Research Article Food Chemistry. 185: 106-111, 2015.
  14. Y. Guo, D. Pan, M. Tanokura. Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Original Research Article Food Chemistry. 114: 328-333, 2009.
  15. K. Hsu, G. Lu, C. Jao. Antioxidative properties of peptides prepared fromtuna cooking juice hydrolysates with Orientase (Bacillus subtilis). Food Research International, 42, 647.65, 2009. https://doi.org/10.1016/j.foodres.2009.02.014
  16. J. Adler-Nissen. Enzymatid hydrolysis of proteins for increased solubility. J Afric Food Chem. 24: 1090-1093, 1976. https://doi.org/10.1021/jf60208a021
  17. D.A. Vattem, R.R. Mahoney. Production of dialyzable iron by in vitro digestion of chicken muscleprotein fractions: the size of the dialyzable iron. J Sci Food Agric, 85, 1537-1542, 2005. https://doi.org/10.1002/jsfa.2043
  18. O. Power, P. Jakeman. R.J. FitzGerald. Antioxidaive peptides: enzymatic production, in vitro and in vivo antioxidant activity and potensial application of milk-derived antioxidative peptides. Ammino Acid,. 44: 797-820, 2013. https://doi.org/10.1007/s00726-012-1393-9
  19. L. You, M. Zhao, J.M. Regenstein, J. Ren. Changes in the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates during a simulated gastrointestinal digestion. Food Chemistry, 120, 810.816, 2010. https://doi.org/10.1016/j.foodchem.2009.11.018
  20. L. You, M. Zhao, J.M. Regenstein, J. Ren. Purification and identification of antioxidative peptides from loach (Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry. Food Research International, 43, 1167.1173, 2010. https://doi.org/10.1016/j.foodres.2010.02.009
  21. J. Ren, M. Zhao, J. Shi, J. Wang, Y. Jiang, C. Cui, Y. Kakuda, S.J. Xue. Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chemistry, 108, 727.736, 2008. https://doi.org/10.1016/j.foodchem.2007.11.010