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Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7 ...
An enzyme's activity decreases markedly outside its optimal temperature and pH, and many enzymes are ... Catalase 7.0 Neutral Urease 7.0 Neutral Cholinesterase 7.0
Optimal pH 7.5 Optimal temperature 37 - 40 °C Catalase activity catalase-negative Utilized sugars glucose, D-xylose, D-mannose, salicin, L-ramnose, and L-arabinose Sugars that cannot be utilized maltose, lactose, trehalose, sucrose, D-sorbitol, raffinose, D-mannitol, melesitol cellobiose Enzymatic activity
Its activity was first identified in 1876 by Frédéric Alphonse Musculus as a soluble ferment. [4] In 1926, James B. Sumner, showed that urease is a protein by examining its crystallized form. [5]
It is positive by the oxidase test and catalase test, but negative by the nitrate reductase test. It is alpha-hemolytic and requires oxygen. A. faecalis can be grown at 37 °C, and forms colonies that lack pigmentation. [1]
The oxidase- and catalase-positive cells are motile and possess lateral/polar flagella. Growth occurs at 10–45 °C (optimally at 25–30 °C) and at pH 5–10 (optimum pH 7–8). The strain is able to grow at salinities between 0 and 25% NaCl (optimum 10–20% NaCl). [2] [3]
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D. donghaensis is able to secrete enzymes such as catalase and oxidase ... although the optimum temperature for growth is 30 °C. The optimal pH for growth is 7–8 ...