• Title/Summary/Keyword: enzymatic hyarolysate

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Angiotensin Converting Enzyme Inhibitory Activity in Enzymatic Hydrolysates of Anchovy Muscle Protein (멸치육 효소 가수분해물의 Angiotensin 전환효소 저해작용)

  • LEE Tae-Gee;PARK Young-Beom;PARK Douck-Choun;YEUM Dong-Min;KIM In-Soo;GU Yeun-Suk;PARK Young-Ho;KIM Seon-Bong
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.875-881
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    • 1998
  • To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive pretenses such as pepsin, trypsin, $\alpha$-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Elavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only $50\%$ ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of $50\%$ ethanol soluble peptide-nitrogen ($ESPN_{50}$). ACE inhibition effects and yield of $ESPN_{50}$ occurred as hydrolysis time increased to 8 hrs, Among those pretenses tested, hydrolysates by Alcalase and $\alpha$-chymohypsin had greater ACE inhibitory activity (80 and $74\%$, reipectively) with eletated levels of $ESPN_{50}$ (48 and 58 mg/ml, respectively), while Protamex hydrolysates had greater ACE inhibitory activities ($73\%$) with reduced levels of $ESPN_{50}$ (7.2mg/ml) than others. Amino acid compositions of $50\%$ ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.

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