2015

RESULT

Table 1: Glucose Standard Curve

Concentration of Glucose (mg/L) | Absorbance (nm) |

100 | 0.20 |

200 | 0.215 |

500 | 0.221 |

1000 | 0.24 |

2000 | 0.251 |

Figure 1: Standard curve calibration

Table 2: Effect of substrate on enzyme activity

Concentration of Substrate (% w/v) | Absorbance (nm) |

0.5 | 0.204 |

1.0 | 0.218 |

2.0 | 0.542 |

3.0 | 0.539 |

Figure 2: Absorbance versus Substrate concentration

Table 3: Effect of pH on enzyme activity

pH Value | Absorbance (nm) |

7 | 0.192 |

8 | 0.28 |

9 | 0.564 |

11 | 0.565 |

Figure 3: Absorbance versus pH

DISCUSSION

Based on Graph 1, the glucose standard calibration curve did follow slightly the theory because graph pattern obtained a linear line in this experiment. Theoretically, when the concentration of glucose increases the enzyme activity also increases. This calibration curve is used as a reference to the substrate and the pH effects towards enzyme activity due to finding its concentration. Meaning that, when an amylase enzyme reacts with substrate starch solution, it will produce glucose. Due to this matter, the glucose standard calibration curve has been used for determining the concentration of glucose after the reaction. The substrate that been used in this experiment is the starch solution, while the enzyme that been used is the amylase enzyme.

Basically, a very small amount of enzyme can consume a large amount of substrate. The rate of reaction depends directly on the amount of enzyme present at a specific time at unlimited substrate concentration. If two folds increase the amount of enzyme the reaction rate is doubled. By increasing the enzyme molecules an increase is the number of active sites takes place. At higher concentration of the enzyme the inhibitors will fall short. More active sites will convert the substrate molecules into products, in the given period of time. After a certain limiting concentration, the rate of reaction...