• Title/Summary/Keyword: Salt-fermented shrimps

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Physicochemical and Sensory Properties of Commercial Salt-Fermented Shrimp (시판새우젓 종류별 이화학적ㆍ관능적 특성)

  • 오상희;성태화;허옥순;방옥균;장해춘;신현수;김미리
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.33 no.6
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    • pp.1006-1012
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    • 2004
  • We evaluated physicochemical and sensory characteristics of 25 commercial salt-fermented shrimps by kind (Oh Jeot, Yook Jeot and Chu Jeot) by manufacturer (traditional marketer (TS) & company (CS)). Salinity and pH ranged 17.9∼28.7% and 7.82∼8.74, respectively, of which Chu Jeot was somewhat higher in salinity and pH, compared with those of the others. Amino nitrogen (AN), volatile basic nitrogen (VBN) and thiobarbituric acid reactive subjects (TBARS) showed great variation ranged with 21.41∼661.13 mg%, 263.2∼1180.2 mg% and 0.507∼1.322 $\mu\textrm{g}$/g, respectively. Hunter color of L value was 53.99∼67.45, a value, 4.98∼12.06 and b value, 4.45∼10.4. Physicochemical quality showed greater variations in Chu Jeot of TS than that of CS. Products of CS have higher salinity while lower VBN and AN than those of TS. Sensory results showed that mean scores of appearance, over-all taste, over-all flavor and over-all acceptability between TS and CS were not significantly different. The mean score of over-all acceptance was the highest in Yook Jeot. Physicochemical and sensory characteristics of salt-fermented shrimps in a PCA plot comprised of first principal component (68.36%) and second principal component (31.36%).

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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