1. Cù Thành Nam 20190525 (C) Lê Văn Đạt 20190313 Nguyễn Đức Lâm 20201034

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technical mid-test writing

Group 9:
Member of team
1. Cù Thành Nam 20190525 (C)
2. Lê Văn Đạt 20190313
3. Nguyễn Đức Lâm 20201034
4. Sroeurn Dalin 20200853
Exercise: Describe a graph of an enzyme

Below is a graph, which discribed the effect of pH on the relative activity of α-amylase. The maximum enzyme activity measured (15.6 U/mL) was established as 100% relative activity, at 55°C with 2% starch as the carbon source.
Looking at the graph, this was an enzyme whose activity is highly dependent on the pH of the medium. From pH 0 - 4, the enzyme was inactivated when the activity reached 0%. From a pH greater than 4, the enzyme started to work. At pH=5, enzyme activity reached about 10%, a relatively low number and unsuitable for enzyme activity. Enzyme activity reached more than 40% at pH = 6, up to 4 times higher than activity at pH = 5. From a pH greater than 6, enzyme activity increased rapidly. About PH = 7, this enzyme activity reached 60%, up to 1.5 times higher than when PH = 6. When the pH reached approximately 8, in a mildly alkaline medium, the enzyme activity peaked at 100%. When the pH of the medium was greater than 8, the enzyme activity decreased gradually. At pH=9, the activity of this enzyme only reached 80% and decreased sharply to 70% when PH=10. At pH=12, enzyme activity decreased to 60%. Enzyme activity decreased to 40% at pH = 13, equal to when pH = 6, only 6.24 U/ml. Through the comments, we saw that this enzyme was very active in neutral to slightly alkaline environment. Through pH analysis, we could apply this enzyme to the hydrolysis process in a neutral or slightly alkaline environment so that the enzyme could work the most effectively

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