저활용 단백질로부터 칼슘 결합물질을 분리하기 위해 돼지 육골분과 진주담치 단백질을 단백질 분해 효소인 alcalase를 이용하여 가수분해물을 제조하였고, 체내 흡수가 용이한 3 kDa 이하로 한외여과 하였다. 돼지 육골분 가수분해물은 Mono Q 컬럼을 통해 분리하였고, 진주담치가수분해물의 경우 Q-Sepharose로 분리 하여 각각 2개, 3개의 peptide fraction을 얻어 각 fraction의 칼슘 결합력을 측정하였다. 그 결과 MBM F2와 Mussel F3에서 가장 높은 칼슘결합력을 나타내었고, 따라서 본 연구 결과로 얻어진 가수분해물들은 칼슘 보충 소재로 활용될 수 있다고 판단된다.

본 연구는 냉동연근의 최적 제조 공정을 위하여 수행하 였다. 냉동 전처리로 blanching 하고, -20, -70, -196℃ 각각 다른 냉동온도에서 동결한 냉동연근의 품질을 측정하였다. 최적 blanching 조건은 미생물 수, 물성, 총 페놀 함량, 관능 평가 등의 결과를 바탕으로, 100℃에서 5분간 처리로 설정 하였다. 여러 냉동조건에서 동결한 연근의 SEM 사진을 비교한 결과, -20℃에서 동결한 연근의 조직이 가장 많이 파괴되었고 –70℃에서 동결한 연근의 조직 단면 구조가 대조구와 가장 유사하였다. 항산화능은 동결 시 감소하는 경향을 나타냈고, 처리구간에 유의적인(p<0.05) 차이는 없 었다. 총 페놀 함량은 모든 냉동연근에서 감소하는 경향을 보였는데 -20℃에서 가장 낮았고, drip loss 또한 -20℃에서 3.73%로 가장 높았다. 따라서 본 연구 결과, -20℃에서의 일반적인 냉동보다는 gas nitrogen convection chamber에서 의 -70℃로 동결하는 것이 고품질의 냉동연근을 생산할 수 있는 최적 냉동방법이라고 판단된다.

As byproducts of chicken slaughtering, chicken feathers are produced and mostly discarded without proper treatment, which results in serious environment pollution. Therefore, the appropriate treatment and utilization of chicken feathers are needed. In particular, chicken feathers can be used as protein sources for the preparation of protein hydrolysates, considering that chicken feathers have a large amount of proteins. In this study, chicken feather protein hydrolysates were prepared and their iron-binding peptides were isolated. Chicken feather protein was extracted from feathers of slaughtered chicken, and its hydrolysates were prepared via hydrolysis with Flavourzyme for 8 h. Then the chicken feather protein hydrolysates were ultra-filtered to obtain small peptide fractions and fractionated using Q-Sepharose and Sephadex G-15 columns to isolate their iron-binding peptides. Two major fractions were produced from each of the Q-Sepharose ion exchange chromatography and the Sephadex G-15 gel filtration hromatography. Among the fractions, the peptide fraction with a high iron-binding activity level, F12, was isolated. These results suggest that chicken feather protein hydrolysates can be used as iron supplements.

Omija (Schizandra chinensis B.) slices were dehydrated with 20, 40, and 60% (w/w) red algae extract (RAE), and 40% of RAE was selected as the proper processing concentration considering the dehydration efficiency and cost of the dehydrating agent. The RAE-treated omija samples were compared with the hot-air dried samples in terms of the qualities such as the rehydration capacity and total phenolic contents. The rehydration ratios of the RAE-treated samples were greater than those of the hot-air dried samples by 31%. The total phenolic contents of the RAE-treated samples (1304.8 mg GAE/100 g) were higher than those of the hot-air dried samples (999.5 mg GAE/100 g). Therefore, omija slices can be dehydrated with RAE without quality loss.

To prepare calcium-binding peptides as calcium supplement, barley proteins were hydrolyzed using Flavourzyme for 18 h and the hydrolysates were ultra-filtered under 3 kDa as a molecular weight. The resultant filtered peptides were fractionated using ion exchange and normal-phase high performance liquid chromatography. Then each fraction that was obtained was determined for its calcium-binding activity to isolate the calcium-binding peptides. As a result, the highest calcium-binding peptide fraction was obtained, and the results suggest that barley protein hydrolysates can be used as a calcium supplement.