Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Optimization of Enzymatic Hydrolysis Conditions for Production of Angiotensin-I Converting Enzyme Inhibitory Peptide from Casein

  • Do, Jeong-Ryong (Korea Food Research Institute) ;
  • Kim, Ki-Ju (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University) ;
  • Kim, Hyun-Ku (Korea Food Research Institute) ;
  • Kim, Young-Myoung (Korea Food Research Institute) ;
  • Park, Yeung-Beom (Department of Food Processing and Bakery, Gangwon Provincial College) ;
  • Lee, Yang-Bong (Department of Food Science and Technology, Pukyong National University) ;
  • Kim, Seon-Bong (Department of Food Science and Technology, Pukyong National University)
  • Published : 2007.08.31
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Abstract

This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

Keywords

References

  1. Manjusri D, Richard LS. Pulmonary angiotensin-converting enzyme. J. Biol. Chem. 250: 6762-6768 (1975)
  2. Cushman DW, Cheung HS. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharm. 20: 1637-1648 (1971) https://doi.org/10.1016/0006-2952(71)90292-9
  3. Webster J, Koch HF. Aspects of tolerability of centrally acting antihypertensive drugs. J. Cardiovasc. Pharma. 3: S49-S54 (1996)
  4. Mullally MM, Meisel H, FitzGerald RJ. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine beta-lactoglobulin. FEBS Lett. 3: 99- 101 (1997) https://doi.org/10.1016/0014-5793(69)80107-9
  5. Miyoshi S, Ishikawa H, Kaneko T, Fukui F, Tanaka H, Maruyama S. Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate. Agr. Biol. Chem. Tokyo 55: 1313- 1318 (1991) https://doi.org/10.1271/bbb1961.55.1313
  6. Matsui T, Matsufuji H, Seki E, Osajima K, Nakashima M, Osajima Y. Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle. Biosci. Biotech. Bioch. 57: 922-925 (1993) https://doi.org/10.1271/bbb.57.922
  7. Do JR. Separation and purification of angiotensin I-converting enzyme inhibitory peptide from mackerel. J. Korean Fish. Soc. 33: 153-157 (2000)
  8. Maruyama S, Miyoshi S, Tanaka H. Angiotensin I converting enzyme inhibitors derived from Ficus carica. Agr. Biol. Chem. Tokyo 53: 2763-2767 (1989) https://doi.org/10.1271/bbb1961.53.2763
  9. Kinoshita E, Yamakoshi J, Kikuchi M. Purificatin and identification of an angiotensin I-converting enzyme inhibitor from soy sauce. Biosci. Biotech. Bioch. 57: 1107-1110 (1993) https://doi.org/10.1271/bbb.57.1107
  10. Ahn CW, Nam HS, Shin JK, Kim JH, Hwang ES, Lee HJ. Effects of gluten and soybean polypeptides on textural, rheological, and rehydration properties of instant fried noodles. Food Sci. Biotechnol. 15: 698-703 (2006)
  11. Pak VV, Koo M, Lee N, Oh SK, Kim MS, Lee JS, Kwon DY. Hypocholesterolemic soybean peptide (LAVP) inhibits HMG-CoA reductase in a competitive manner. Food Sci. Biotechnol. 14: 727- 731 (2005)
  12. Maruyama S, Suzuki H. A peptide inhibitor of angiotensin I converting enzyme in the tryptic hydrolysate of casein. Agr. Biol. Chem. Tokyo 46: 1393-1394 (1982) https://doi.org/10.1271/bbb1961.46.1393
  13. Yamamoto N, Akino A, Takano T. Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790. J. Dairy Technol. 77: 917-922 (1994)
  14. Maruyama S, Mitachi H, Awaya J, Kurono M, Tomizuka N, Suzuki H. Angiotensin I-converting enzyme inhibitory activity of the Cterminal hexapeptide of ${\alpha}s_1$-casein. Agr. Biol. Chem. Tokyo 51: 2557-2561 (1987) https://doi.org/10.1271/bbb1961.51.2557
  15. SAS Insitute, Inc. SAS User's Guide. 2nd ed. Academy of Freedom. Statistical Analysis System Institute, Cary, NC, USA (1992)
  16. Kim HS, In YM, Jeong SG, Ham JS, Kang KH, Lee SW. Angiotensin I-converting enzyme inhibitory properties of bovine casein hydrolysates in different enzymatic hydrolysis conditions. Korean J. Food Sci. Anim. Resour. 22: 87-93 (2002)
  17. Yoon S, Choi HJ, Lee JS. Modification of functional properties of casein by kiwifruit protease. Korean J. Food Sci. Technol. 7: 93-101 (1991)
  18. Yoon JH, Yoon JO, Hong KW. Fractionation of angiotensin converting enzyme (ACE) inhibitory peptide from casein hydrolysates by proteases. Food Eng. Prog. 7: 116-120 (2003)