Extraction of Invertase from Yeast
EXTRACTION OF INVERTASE FROM YEAST
AND EFFECT OF pH ON ENZYMATIC ACTIVITY
Jenelle C. Faustino, John Gambit B. Garcia, Fatima S. Jusay,
Oliver Alexander B. Lao and Eunice L. Licudine
Group 4 2 E Medical Technology Biochemistry Laboratory
ABSTRACT
Enzymes are substances that are produced by living organisms and act as catalysts in order to speed up or chance a chemical reaction without changing itself at the end of the reaction. Invertase was extracted first from baker’s yeast. Determination of the effects of changes in pH on enzymatic activity was the main objective of this experiment. Dinitrosalicylic acid (DNS) colorimetric method was used in determining the enzymatic activity of invertase. Invertase was then mixed in different buffer solutions of varying pH. After subjecting the enzyme to the different buffers, absorbance of the invertase was measured under 540 nm using a spectrophotometer.
Invertase was subjected to different PH of buffer solution and was observed under 540 nmabsorbance using spectrophotometer. After observation and analysis, a peak was observed by plotting absorbanceversus ph and was known as optimum PH. Optimum PH is said to be the most favorable PH value or the point wherethe enzyme is most active. And that invertase exhibits high activity over a broad PH range of 3.5 – 5.5 with optimumPH near 4.5. But due to human errors, the acquired data was incorrect giving an unreliable basis for thedetermination of the effect of PH on enzymatic activity
INTRODUCTION Enzymes are biological catalysts which speed up chemical reactions by lowering the activation energy, the energy required to break bonds. [1] Enzymes are also affected by factors such as temperature, cofactors, activators, inhibitors, and pH. Invertase, also known as β-D-Fructofuranoside fructohydrolase [2], is a glycoprotein which contains 50% mannan and 2-3% glucosamine. Invertase also can break peptide bonds. It hydrolyzes sucrose to produce glucose and
AND EFFECT OF pH ON ENZYMATIC ACTIVITY
Jenelle C. Faustino, John Gambit B. Garcia, Fatima S. Jusay,
Oliver Alexander B. Lao and Eunice L. Licudine
Group 4 2 E Medical Technology Biochemistry Laboratory
ABSTRACT
Enzymes are substances that are produced by living organisms and act as catalysts in order to speed up or chance a chemical reaction without changing itself at the end of the reaction. Invertase was extracted first from baker’s yeast. Determination of the effects of changes in pH on enzymatic activity was the main objective of this experiment. Dinitrosalicylic acid (DNS) colorimetric method was used in determining the enzymatic activity of invertase. Invertase was then mixed in different buffer solutions of varying pH. After subjecting the enzyme to the different buffers, absorbance of the invertase was measured under 540 nm using a spectrophotometer.
Invertase was subjected to different PH of buffer solution and was observed under 540 nmabsorbance using spectrophotometer. After observation and analysis, a peak was observed by plotting absorbanceversus ph and was known as optimum PH. Optimum PH is said to be the most favorable PH value or the point wherethe enzyme is most active. And that invertase exhibits high activity over a broad PH range of 3.5 – 5.5 with optimumPH near 4.5. But due to human errors, the acquired data was incorrect giving an unreliable basis for thedetermination of the effect of PH on enzymatic activity
INTRODUCTION Enzymes are biological catalysts which speed up chemical reactions by lowering the activation energy, the energy required to break bonds. [1] Enzymes are also affected by factors such as temperature, cofactors, activators, inhibitors, and pH. Invertase, also known as β-D-Fructofuranoside fructohydrolase [2], is a glycoprotein which contains 50% mannan and 2-3% glucosamine. Invertase also can break peptide bonds. It hydrolyzes sucrose to produce glucose and