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http://dx.doi.org/10.5657/kfas.2006.39.3.269

Improving the Functional Properties of Oyster Hydrolysates by Two-step Enzymatic Hydrolysis  

Chung In-Kwon (Division of Marine Life Science, Institute of Marine Industry, Gyeongsang National University)
Kim Jin-Soo (Division of Marine Life Science, Institute of Marine Industry, Gyeongsang National University)
Heu Min-Soo (Division of Marine Life Science, Institute of Marine Industry, Gyeongsang National University)
Publication Information
Korean Journal of Fisheries and Aquatic Sciences / v.39, no.3, 2006 , pp. 269-277 More about this Journal
Abstract
This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.
Keywords
Oyster hydrolysates; Oyster; Two-step enzymatic hydrolysis; ACE inhibitory activity; Antioxidant activity; Antimicrobial activity;
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1 Byun, H.G. and S.K. Kim. 2001. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Proc. Biochem., 36, 1155- 1162
2 Li, Q., M. Osada and K. Mori. 2000. Seasonal biochemical variations in Pacific oyster gonadal tissue during sexual maturation. Fish. Sci., 66, 502-508   DOI   ScienceOn
3 Ministry of Social Welfare of Japan. 1960. III. Volatile basic nitrogen. In: Guide to Experiment of Sanitary Infection. Kenpakusha, Tokyo, 30-32
4 Mitsuda, H, K. Yasumoto and K Iwami. 1996. Antioxidative action of indole compounds during the autoxidation of linoleic acid. Eiyoto Shokuryo, 19, 210-214
5 NFRDA. 1995. Supplemented Chemical Composition of Marine Products in Korea. National Fisheries Research and Development Agency, Yemoon Publishing Co., Seoul, Korea, 139-143
6 Shiau, C.Y. and T. Chai. 1990. Characterization of oyster shucking liquid wastes and their utilization as oyster soup. J. Food Sci., 55, 374-378   DOI
7 Soudant, P. and F.L. Chu. 2001. Lipid class and fatty acid composition of the protozoan parasite of oysters, Perkiasus mariaus cultivated in two different media. J. Eukary. Microbiol., 48, 309-319   DOI   ScienceOn
8 Steel, R.G.D. and J.H. Torrie. 1980. Principle and Procedures of Statistics. McGraw-Hill Kogakusha, Tokyo, 187-221
9 Yoon, H.D., H.S. Byun, S.J. Chun, S.B. Kim and Y.H. Park. 1986. Lipid composition of oyster, arkshell and sea-messel. J. Kor. Fish. Soc.. 19. 321-326
10 Heu, M.S. and S.H. Ahn. 1999. Development and fractionation of proteolytic enzymes from inedible seafood product. J. Kor. Fish. Soc., 32, 458-465   과학기술학회마을
11 Hosoi, M., S. Kubota, M. Toyohara, H. Toyohara and I. Hayashi. 2003. Effect of salinity change on free amino acid content in Pacific oyster. Fish. Sci., 69, 395-400   DOI   ScienceOn
12 Davison, P.M. and M.E. Parish. 1989. Methods for testing the efficacy of food antimicrobials. Food Technol., 1, 148
13 Hazato, T. and R. Kase. 1986. Isolation of angiotensin I converting enzyme inhibitor from porcine plasma. Biochem. Biophys. Res. Commun., 139, 52-55   DOI   ScienceOn
14 Horiuchi, M., K.I. Fujimura, T. Terashima and T. Iso. 1982. Method for determination of angiotensin-converting enzyme activity in blood and tissue by high-performance liquid chromatography. J. Chromatogr., 233, 123-130   DOI   ScienceOn
15 Jeon, Y.J., H.G. Byun and S.K. Kim. 1999. Improvement of functional properties of cod frame protein hydrolysates using ultrafilteration membranes. Proc. Biochem., 35, 471-478
16 Jeong, B.Y., B.D. Choi and J.S. Lee. 1998. Proximate composition, cholesterol and $\alpha$-tocopherol content in 72 species of Korean fish. J. Kor. Fish. Sci. Tech., 1, 129-146
17 Kim, C.Y. J.H. Pyeun and J.N. Nam. 1981. Decomposition of glycogen and protein in pickled oyster during fermentation with salt. J. Kor. Fish. Soc., 14, 66-71   과학기술학회마을
18 Kim, J.S. and M.S. Heu. 2001. Preparation of instant powdered soup using canned oyster processing waste water and its characteristics. J. Kor. Fish. Soc., 34, 285-290
19 Kim, J.S., D.M. Yeum, H.G. Kang, I.S. Kim, C.S. Kong, T.G. Lee and M.S. Heu. 2002. Fundamentals and Applications for Canned Foods. Hyoil Publishing Co., Seoul, Korea, 321-325
20 Kim, S.K., H.G. Byun, P.J. Park and F. Shahidi. 2001a. Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J. Agric. Food Chem., 49, 2992-2997   DOI   ScienceOn
21 Kim, S.K., Y.T. Kim, H.G. Byun, K.S. Nam and F. Shahidi. 2001 b. Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin. J. Agric. Food Chem., 49, 1984-1989   DOI   ScienceOn
22 AOAC. 1995. Official Methods of Analysis. 16th ed. Association of Official Analytical Chemists, Washington DC., 69-74
23 Cook, D.W., T. Chai, C.R. Hackney, R.E. Martin, W.S. Otwell and D.R. Ward. 1988. Liquid loss in shucked oyster (Crassostrea virginica) meats during ice storage. J. Food Sci., 53, 1671-1683   DOI
24 Astawan, M., M. Wahyuni, T. Ysauhara, K. Yamada, T. Tadokoro and A. Maekawa. 1995. Effects of angiotensin I converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats. Biosci. Biotech. Biochem., 59, 425-429   DOI   ScienceOn
25 Cheung, H.S., F.L. Wang, M.A. Ondetti, E.F. Sabo and D.W. Cushman. 1980. Binding of peptide substrates and inhibitors of angiotensin I converting enzyme. Importance of the COOH-terminal dipeptide sequence. J. Biol. Chem., 255, 401-407