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Postmortem Changes of the Protein and Amino Acid Composition of Muscles in the Partially Frozen Prawn, Pandalus japonica (보리새우육의 부분동결저장중 단백질 및 아미노산의 조성변화)

  • PYEUN Jae-Hyeung;CHOI Young-Joon;KIM Jeung-Han;CHO Kweon-Ock
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.17 no.4
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    • pp.280-290
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    • 1984
  • An extensive study has been made on the relationship between the freshness and the compositions of the muscle protein of prawn, Pandalus japonica during the storage under partially frozen condition. The variations of the subunit distribution for sarcoplasmic protein and myofibrillar protein extracted from the samples by changes of freshness were discussed by sodium dodecylsulfate-poly-acrylamide gel (SDS-PAG) electrophoresis. On the other hand, the denaturation constant ($K_D$) of the myofibrillar protein extracted from the prawn stored at $-3^{\circ}C\;and\;-20^{\circ}C$ were successively compared. The prawn muscle contained about $18\%$ of protein with the composition of $32\%$ in sarcoplasmic protein, $56\%$ in myofibrillar protein, $10\%$ in residual intracellular protein and $2\%$ in stroma. The indices for estimating freshness of the muscle were approached to the early stage of putrefaction on the 26th day of the storage with $25.29mg\%$ of total volatile basic nitrogen, $31.36\%$ of K-value and 8.83 of pH. The content of the myofibrillar protein was remarkably decreased with the time during the storage while that of residual intracellular protein was increased. The $K_D$ values of the myofibrillar protein were $9.03{\times}10^{-6}sec^{-1}\;at\;-3^{\circ}C\;and\;4.42{\times}10^{-6}sec^{-1}\;at\;-20^{\circ}C$. The results of the analysis of SDS-PAG electrophoretograms indicated that the sarcoplasmic protein and the myofibrillar protein were composed of 12 subunits and 17 subunits in the muscle of instantaneously killed prawn ana were changed into 8 subunits and 22 subunits in the muscle stored for 26 days, respectively. It is noticeable that 30,000, 41,000, 107,000, 136,000, 170,000 173,000, 185,000, and 198,000 daltons of the newly appeared 8 subunits were found in the myofibrillar protein from the prawn muscle stored for 26 days. The amino acid composition of the muscle protein showed that the most of amino acids were slightly decreased with the days of the storage. With respect to the free amino acid composition of the muscle of instantaneously killed prawn, glycine, proline, arginine, alanine and taurine comprised $93\%$ of the total free amino acids. Taurine, valine, leucine, phenylalanine, serine, lysine, methionine, isoleucine and histidine were increased during the storage period but exceptionally proline was decreased.

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Processing of Water Activity Controlled Fish Meat Paste by Dielectric Heating 1. Formulation and Processing Conditions (내부가열을 이용한 보장성어육(고등어) 연제품의 가공 및 제품개발에 관한 연구 1. 원료${\cdot}$첨가물의 배합 및 가공조건)

  • LEE Kang-Ho;LEE Byeong-Ho;You Byeong-Jin;SUH Jae-Soo;JO Jin-Ho;JEONG In-Hak;JEA Yoi-Guan
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.17 no.5
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    • pp.353-360
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    • 1984
  • As an effort to expand the utilization of mackerel which has been thought disadvantageous to processors due to the defects in bloody dark color of meat, high content of lipid, and low stability of protein, and to develope a new type of product, so called, preservative fish meat paste, the processing method was studied in which dielectric heating was applied by means of cooking, pasteurization, dehydration, and control of water activity. The principle of this method is based on that dielectric heating can initiate a rapid dispersion or displacement of moisture in the meat tissue so that the level of water acivity can be controlled by dehydration with hot air meanwhile the product is cooked, pasteurized, and texturized. And the product is finally heated with electric heaters and vacuum sealed to stabilize water activity and storage stability. In present paper, a formula for preparing the fish meat-stach paste, the conditions of dielectric heating and dehydration, shape and size of the product, and other parameters were tested to optimize the process operation. A formula of the fish meat-starch paste to provide proper textural properties and water activity was $10\%$ starch, $1.5\%$ salt, $3\%$ soybean, $0.6\%$ MSG, $2\%$ sucrose, and $3\%$ sorbitol against the weight of fish meat. A proper shape and size of the product to avoid foaming and case hardening during heating was sliced disc of 8 cm $diameter{\times}0.8$ cm thickness or $10{\times}10$ cm square plate with 1.0 cm thickness. The disc shape was recommended because it resulted more uniform heating, minimum foaming and case hardening. And it was also advantageous that disc was simply provided when the fish meat disc was stuffed in the same, solidified in boiling water for 2 to 3 minutes, and sliced. Condition of dielectric heating was critical to decide the levels of sterility, water activity, and textural property of the product. The temperature at the center of the meat disc slices was raised up to $95^{\circ}C$ in 1.5 minutes so that continuous exposure to microwave caused expanded tissue and hardening ending up with a higher water content. Heating for 5 to 6 minutes was adequate to yield the final water activity of 0.86 to 0.83(35 to $40\%$ moisture). It is important, however, that heating had to be done periodically, for instance, in the manner of 2.0, 1.5, 1.5, and 1.0 minute to give enough time to displace or evaporate moisture from the meat tissue. The product was dehydrated for 2 to 3 minutes by hot air of $60^{\circ}C$, 3 to 5m/sec and finally exposed to electric heaters for 5 to 6 minutes until the surface was roasted deep brown. These conditions of heating and dehydration resulted in a complete reduction of total plate count from an initial count of $5.3{\times}10^6/g$ to less than $3{\times}10^2/g$. General composition of the product was $40.1\%$ moisture, $20.8\%$ protein, $17.4\%$ lipid, $16.2\%$ carbohydrate, and $5.5\%$ ash. Textural properties revealed folding test AA, hardness 42, cohesiveness 0.53, toughness 4.6, and elasticity 0.8.

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