Proteinases Contained in Cheeses Imported from Denmark and Germany

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  • デンマークおよびドイツから輸入されたチーズ中のプロティナーゼ
  • デンマーク オヨビ ドイツ カラ ユニュウサレタ チーズチュウ ノ プロティナ

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Proteinases contained in 4 types of cheese imported from Denmark and Germany (Samsoe and Maribo cheese from Denmark and Tilsit and Trapist cheese from Germany) were separated by using CM-Sephadex. As a result, 3 proteinases were eluted from each cheese sample at salt concentrations of 0.3, 0.6, and 0.8-0.9M. Regarding each proteinase, the optimum pH, effects of various reagents and action on casein were examined. Consequently, proteinases eluted at the same salt concentration showed the same properties. Thus they were refferred to as the same enzyme. The proteinase eluted at 0.3M showed the maximum activity at pH 3.8 to 4.0 and was completely inactivated with pepstatin. It quickly decomposedκ-casein to thereby give a para κ-casein-like decomposition product. The proteinase eluted at 0.6M showed the maximum activity at pH 4.0 and was completely inactivated by pepstatin. It quickly decomposed κ-casein to thereby give a substance being the same asαs1-I casein, β-I and para κ-casein in mobility.The properties of these enzymes suggest that they are milk coagulating enzymes employed at the early stage of cheese making. The properties of the latter enzyme are identical with those of chymosin which is a milk coagulating enzyme. The proteinase eluted at 0.8-0.9M had the optimum pH of around 8.0 and was strongly inhibited by soybean trypsin inhibitor and diisopropyl fluorophosphate. It formed a γ-casein-like decomposition product. These properties agree with those of milk alkaline proteinase.

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