초록
Papain, pepsin, $\alpha-chymotrypsin$ 및 protease을 이용하여 말쥐치육 단백질의 pepsin가수분해물로 부터 합성한 plastein과 유리 glutamic acid 및 leucine을 도입시킨 plastein의 일반성분, 아미노산조성, 분자량, 색조 및 IR spectrum을 측정하여 비교 검토한 결과를 요약하면 다음과 같다. Plastein의 단백질함량은 $76.4\~79.0\%$였으나 protease plastein만이 $72.4\%$로 다소 낮았으며, 회분함량은 $7.4\~11.8\%$로 Glu-papain plastein과 Leu-papain plastein의 $3.9\%$ 및 $4.1\%$보다 높았고, 지방 함량은 $0.3\~0.9\%$ 범위였다. 수율은 papain plastein이 $55\%$로 가장 높았고, pepsin plastein, $\alpha-chymotrypsin$ 및 pretense plastein은 각각 $47.6\%,\;38.3\%,\;23.6\%$ 였으며, Glu-papain plastein과 Leu-papain plastein은 각각 $35.0\%,\;45.7\%$ 였다. Plastein 종류에 따른 아미노산조성에는 큰 차이는 없었으며, Glu-papain plastein과 Leu-papain plastein의 glutamic acid 및 leucine함량은 각각 $38.7\%,\;41.7\%$였으나 대조구인 papain plastein에서는 이들의 함량이 $14.0\%,\;10.1\%$에 불과하였다. Gel여과법에 의한 가수분해물의 분자량은 2,000 및 310인 것이 주종을 이루었으나 이외에도 분자량이 1,600 및 120인 획분도 존재하였다. Plastein의 분자량은 papain plastein이 21,000 및 4,900 였으며, pepsin plastein 24,000, $\alpha-chymotrypsin$ plastein 18, 500, protease plastein 6,700, Glu-papain plastein 24,000, Leu-papain plastein은 17,000 이었다. IR spectrum상에서는 동결건조육, FPC및 가수분해물간에 거의 차이가 없었다.. 그러나 plastein의 경우는 이들과 달리 $800\~850\;cm^{-1},\;700\~750\;cm^{-1} 및 $600\~700\;cm^{-1}$에서 강한 흡수띠가 나타났지만 protease plastein만이 흡수띠가 비교적 약하였다. Glu-papain plastein은 amide I의 흡수띠가 넓게 퍼진 반면에 $1,440cm^{-1}$에서 새로운 흡수띠가 나타났다. 그러나 Leu-papain plastein의 경우는 특징적인 흡수띠가 나타나지 않았다.
In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of filefish protein. Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, pepsin, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper). Also, L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. And, General composition, yield, molecular weight, amino acid composition, color and IR spectrum of plasteins were measured. The protein, ash and lipid content of the plasteins were $72\~78\%,\;7.4\~11.8\%\;and\;0.3\~0.9\%$ respectively. The yield of plasteins were papain $55.0\%,\;pepsin\;47.6\%,\;\alpha-chymotrypsin\;38.3\%,\;protease\;23.6\%$, glutamic acid-incorporated plastein (Glu-Plastein) $35.0\%$, and leucine-incorporated plastein (Leu-plastein) $45.7\%$. The glutamic acid and leucine content in Glu-plastein and Leu-plastein were $38.7\%,\;41,7\%$, respectively, while the contents in the peptic filefish protein hydrolysate were $16.01\%\;and\;8.16\%$, respectively. The amino acid compositions were similar to that of the original filefish muscle protein. The major molecular weights of the peptic hydrolysate estimated by gel filteration were 2,000 and 310, and those of plasteihs were 21,000 and 4,900 for papain, 24,000 for pepsin, 18,500 for $\alpha-chymotrypsin$ 6,700 for protease, 24,000 for Glu-plastein and 17,000 for Leu-plastein. The structural changes in freeze-dried filefish meat, the FPC and hydrolysate were not observed on the IR spectrum. But plasteins showed amide I band in $1,600\~l,700cm^{-1}$ range and resulted in a strong band in $800\~850\;cm^{-1},\;700\~750\;cm^{-1}\;and\;650\~700\;cm^{-1}$. The amide I band of Glu-plastein was wider than those of other plasteins and had also a small band at $1,440\;cm^{-1}$.