• Title/Summary/Keyword: salf-fermented shrimp

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Identification of Aroma-Active Compounds in Korean Salt-Fermented Fishes by Aroma Extract Dilution Analysis 2. Aroma-Active Components in Salt-Fermented Shrimp on the Market (AEDA법에 의한 한국한 젓갈류의 Aroma-Active 성분의 구명 2. 시판 새우젓의 Aroma-Active 성분)

  • Cha, Yong-Jun;Kim, Hun;Jang, Sung-Min;Park, Jee-Young
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.28 no.2
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    • pp.319-325
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    • 1999
  • Volatile flavor compounds in Korean salt fermented shrimp on the market were analyzed by vacuum simultaneous distillation solvent extraction/gas chromatography/mass spectrometry/olfac tometry(V SDE/GC/MS/O) and aroma extract dilution anlaysis(AEDA). A total of 32 volatile com pounds were detected by GC/O analysis. Of these, 18 were positively identified, and composed of S containing compounds(5), aldehydes(4), ketones(3), N containing compounds(3), ester(1), alcohol(1) and aromatic hydrocarbon(1). Predominant odorants(Log3FD$\geq$4) in salt fermented shrimp were 2,3 butanedione(sour/buttery), 1 octen 3 one(earthy/mushroom like), dimethyl trisulfide(cooked cabbage /soy sauce like) and 2 acetylthiazole(grainy/nutty). Predominant free amino acids were aspartic acid, glutamic acid(sour and umami taste), arginine, methionine(bitter) and lysine(sweet and bitter) in evaluation of taste value.

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Purification and Characterization of Extracellular Lipase from Staphylococcus xylosus SC-22 (Staphylococcus xylosus SC-22가 생산하는 lipase의 정제 및 특성)

  • 성찬기;갈상완;이상원;최영주
    • Journal of Life Science
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    • v.11 no.5
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    • pp.457-463
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    • 2001
  • A bacterial strain SC-22 which produced alkaline lipase was isolated from salf-fermented shrimps. Strains SC-22 was identified as Staphylococcus xylosus. An alkaline lipase excreted by Staphylococcus xylosus SC-22 was purified by ammonium sulfate predipitation and column chromatography on Sephadex G-100 and DEAE-Sephace. The specific activity of purified lipase was 756U/mg of protein with 17.2% yield. The approximate molecular weight of the purified enzyme was 47 kDa. The partially purified lipase preparation had and optimum temperature of 4$0^{\circ}C$, an optimum pH of 8.0, and a stable of 5~10. Lipase activities were enhanced by salt ions such as $Ca^{2+}$, $Mg^{2+}$,N $a^{2+}$ while inhibited remarkably by heavy metal ions, C $u^{2+}$ and P $b^{2+}$.EX> 2+/.

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