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곽해수,Chogsom Chimed,유상훈,장윤혁 한국축산식품학회 2016 한국축산식품학회지 Vol.36 No.2
The objective of this study was to determine the physicochemical and sensory properties of Appenzeller cheese supplemented with different concentrations (0, 1, 2, 3, and 4%, w/w) of powdered microcapsules of tomato extracts (PMT) during ripening at 14°C for 6 mon. The particle sizes of PMT ranged from 1 to 10 m diameter with an average particle size of approximately 2 m. Butyric acid (C4) concentrations of PMT-added Appenzeller cheese were significantly higher than that of the control. Lactic acid bacteria counts in the cheese were not significantly influenced by ripening time from 0 to 6 mon or the concentrations (0-4%, w/w) of PMT. In terms of texture, the hardness of PMT-added Appenzeller cheese was significantly increased compared to the control. The gumminess and chewiness of PMT-added Appenzeller cheese were similar to those of the control. However, both cohesiveness and springiness of PMT-added Appenzeller cheese were slightly decreased. In sensory analysis, bitterness and sourness of Appenzeller cheese were not significantly changed after supplementation of PMT, but sweetness of the cheese was significantly increased after increasing the ripening time from 0 to 6 mon and increasing the concentration from 1 to 4% (w/w). Based on these results, the addition of the concentrations (1-4%, w/w) of PMT to Appenzeller cheese can be used to develop functional Appenzeller cheese.
숙성 중 체다치즈에서 분리한 Pseudomonas fluorescens SDR901 의 단백질분해 효소의 특성
곽해수,이경욱,신용국 한국낙농학회 1992 韓國酪農學會誌 Vol.14 No.2
체다치즈의 숙성촉진을 위한 우수한 형질의 단백질분해효소를 선발하기위하여 숙성 중 체다치즈에 존재하는 Pseudomonas fluorescens SDR901로 부터 분리한 단백질분해효소의 특성을 연구하였다. P. fluorescens SDR901이 생산하는 단백질분해효소는 Sephadex G-100 gel filtration으로 부분정제한 결과 220㎖∼270㎖ elution volume에서 용출되었으며, 분자량은 47,900이었다. 효소 분리시 최종 회수율은 17.924%이었으며, 단백질분해효소는 alkaline protease로서 반응최적조건이 pH 9.5, 40℃이었다. 효소의 활력은 Mn^(2+)에 의해 2배로 증가한 반면 Fe^(3+)에 의해서는 1/4로 감소되었다. 단백질 분해효소에 의한 casein의 분해시 초기에는 α_(s1)-casein과 β-casein이 분해되어 α_(s1)-I-peptide와 γ-casein이 증가한 반면 반응시간이 경과함에 따라 α_(s1)-casein, α_(s1)-I-peptide, α_(s2)-casein 및 β-casein은 감소하고 peptide fragment는 증가되었다. The characteristics of protease isolated from Pseudomonas fluorescens SDR901 being in Cheddar cheese during ripening was studied to select a superior protease for acceleration of ripening Cheddar cheese. This protease was eluted between 220㎖ and 270㎖ during purification by the Sephadex G-100 gel filtration, and the molecular weight was 46,900. The final yield of this protease was 17.924%. The optimum pH and temperature for the reaction of this protease were pH 9.0 and 40℃, so this protease was an alkaline protease. The protease activity increased doubly by Mn^(2+), but it decreased to one fourth by Fe^(3+). When casein was hydrolyzed by this protease, α_(s1)-I-peptide and α_(s1)-casein increased with the break up of α_(s1)-casein and β-casein at early stage of hydrolysis, but as reaction proceeded, α_(s1)-casein, α_(s1)-I-peptide, α_(s2)-casein and β-casein decreased with the increase of peptide fragments.
Model system 을 이용한 Mozzarella Cheese 의 이화학적 특성
곽해수,이부웅,정은자 한국낙농학회 1992 韓國酪農學會誌 Vol.14 No.4
Mozzarella caseinate는 용해도, 수화성, 유화능 이 Camembert caseinate보다 우수한 것으로 나타났다. 두 caseinate간에 Ca 고정능력에 차이는 없었으나 Ca에 대한 감수는 Mozzarella보다 Camembert가 높게 나타났다. 소화 효소에 대한 감수성도 Mozzarella가 약간 높았다. Mozzarella caseinate는 140℃에서 25분 가열해야 침전되어 Camembert 보다 높은 열안정성을 나타내었으나 UV spectrum과 산 염기 적정에서 변화가 인정되지 않았다. 전자 현미경 사진에서 용액의 입자의 크기는 두 caseinate가 비슷하나 Na-caseinate보다 훨씬 거대하였다. 신속 해교 측정에서 Mozzarella caseinate는 수화성과 염색이 높았는데 이러한 변화는 모두 kneading과 streching에서 유래되는 것으로 보인다. 치즈의 생화학적 특성을 연구하는데 Model system의 이용은 유익하게 될 것으로 사료된다. 감사의 글 이 논문은 1991년도 학술 진흥재단의 지방대육성연구비로 수행되었고 실험의 일부분은 서울우유기술연구소도 참여하였고 전북대학교 축산과 이광숙양과 김신형군의 치즈제조 및 분석에 관한 노고에 감사를 표시한다. This study was carried out to investigate the physicochemical characteristics of Mozzarella cheese by comparing of caseinate in Camembert and Mozzarella cheese. The result of this study showed that Mozzarella caseinate was superior to Camembert caseinate in solubility, hydration, emulsification. There was no difference in fixing capacity for Ca between the two caseinate, but in case of sensitivity for Ca, Camembert was higher than Mozzarella. And in case of sensitivity for digestive enzyme, Mozzarella was a little higher than Camembert, too. After applying heat of 140℃ for 25 minutes, Mozzarella caseinate showed better heat stability than Camembert, but there was no change in U V spectrum, acid-base titration. Through the electronic microphotograph, we found that there was no difference in liquid particle sizes between them, but they were bigger than Na-caseinate. But Mozzarella caseinate showed good hydration and viscosity in the course of rapid peptization evaluation. And all those changes were seemed to be derived from kneading and stretching. The model system was thought to be useful for the study of biochemical characteristics of cheese.