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Cellulase의 利用에 關한 硏究 : 第 1 報 大豆蛋白의 抽出에 對하여 Ⅰ. On the extraction of the soybean protein
金明燦,成洛癸,奇宇京 진주농과대학 1969 진주농과대학 연구논문집 Vol.- No.8
絲狀菌 Cellulase의 食品加工에의 利用의 一環으로 大豆와 비지에 對하여 Protein의 抽出試驗을 하였으며 實地 豆腐製造에 利用하여 다음과 같은 結果를 얻었다. 1) 本實驗室에서 製造한 Trichoderma 劑 酵素는 大豆와 비지에 對하여 Protein 抽出率이 높았다. 2) Trichoderma 酵素에 混在하는 大部分의 Protease는 熱處理(60℃30分)에 依하여 Cellulase component의 많은 失活없이 除去되었다. 3) 熱處理한 同 Trichoderma Cellulase를 使用하여 大豆와 비지로 부터 豆腐를 만들어 顯著한 收量 增加를 얻었다. As the part of the utilization of celluloytic enzyme derived from Trichoderma viride to the food processing, the extractability of the protein from soy bean and soy bean refuse was studied and some practical point in the preparoion of the soy bean curd was investigated. The results obtained were summerized as follows: 1) The crude enzyme from Tricoderma viride prepared in our laboratory had high extractability of protein from both soy bean and soy bean refuse. 2) Most of protease from Trichoderma viride was eliminated with little loss of celluloytic activity by heat treatment. 3) The increased yield of soy bean curd from soy bean refuse or soy bean was obtained using heat treated crude enzyme.
고도 호열성균 Thermus caldophilus의 Adenylate Kinase의 성질
기우경,太田隆久 한국산업미생물학회 1990 한국미생물·생명공학회지 Vol.18 No.5
내열성 Thermus caldopilus로부터 정제된 내열성의 adenylate kinase는 nucleoside monophosphate에 대해 nucleotide triphosphate보다 높은 기질 특이성을 보여 주었다. P', P^5-di(adenosine-5') pentaphosphate는 여러 기질에 있어 Thermus의 adenylate kinase에 대해 경쟁적 저해제로서 작용하였다. Mg^2+ 이외 여러 가지 2가 양이온은 Ca^2+, Mg^2+, Ba^2+, Fe^2+ 순위로 효소활성에 필요하였으며, 효소활성은 p-choloromucuribenzoic acid와 같은 sulfurhydryl 시약에 저해되지 않았으며, 식염이나 phosphenolpyruvate을 반응액에 첨가하였을 때 활성화되었다. A thermostable adenylate kinase isolated from the sonic extracts of Thermus caldophilus cells revealed higher substrate-specificity to the nucleoside monophosphate than to the nucleoside triphosphate. A p1, p5-di(adenosine-5')pentaphosphate was acted as a competitive inhibitor to the various substrates. Various divalent cations were activated the enzyme activity following orders: Mg^2+, Ca^2+, Mn^2+, Ba^2+, and Fe^2+. The enzyme activity was not affected by the sulfurhydryl reagent, p-chloromeric uribenzoic acid and activated by addition of the sodium chloride or phosphoenol pyruvate to the reaction mixture.