一好塩性細菌の静菌液の酵素作用に対する食塩濃度の影響について

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  • イチ コウエンセイ サイキン ノ セイキンエキ ノ コウソ サヨウ ニ タイスル ショクエン ノウド ノ エイキョウ ニ ツイテ
  • Effect of Sodium chloride on the Enzyme Actions of Cell Suspension of a Halophile, Vibrio sp. No. 10

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Vibrio sp. No. 10. Moderate Halophileの静菌液の酵素作用に対する食塩濃度の影響を見た.1)葡萄糖,乳酸,クエン酸及びコハク酸等を酸化し,この内葡萄糖及び乳酸の脱水素作用は4%NaClで最大であつたが,クエン酸及びコハク酸は低濃度食塩程その作用が強かつた.2)ロイシン,ヴアリン,アラニン及びアスパラギン酸等を脱アミノしたがその作用は弱くロイシンは比較的強かつた.6%NaClにおけるロイシン脱アミノ作用の至適pHは8.5附近にあり,又その至適食塩濃度は培養食塩濃度により影響された.3)静菌液のロイシン脱アミノ及び葡萄糖脱水素作用は低濃度食塩よりも6%NaClに於て安定であり,殊にロイシン脱アミノ作用は1%NaClに於て速かにその作用が低下した.

A general survey has been made of the enzyme actions on a moderate halophile with considerable high salt requirements. The cell suspension of the test organism was able to oxidize glucose, citrate and succinate. The ability to oxidize glucose and lactate was most active in 4% NaCl solution, while a capacity to use succinate and citrate was gradually decreased by increasing the concentration of NaCl. This organism also shows to deaminate weakly the amino acids (alanine, valine, aspartic acid and leucine), but the activities of amino acid deamination varied in accordance with the change in the concentration of NaCl in the reaction mixture and with the amino acid tested as substrate. Leucine was deaminated higher than the other amino acids and its optimum pH of deamination was about pH 8.5. Enzyme activities of the cell suspension on glucose or leucine were more stable in 6% NaCl than in a low concentration of it. Leucine deaminase was unstable and the activity against this amino acid decreased rapidly in 1% NaCl.

長崎大学水産学部研究報告, v.7, pp.117-121; 1959

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