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Stability and kinetic study of serine protease from exocarp of Benincasa Hispida / Siti Syarrah Mohammad Hanapiah

By:

Siti Syarrah Mohammad Hanapiah

Material type: Text

TextPublication details: Kuantan, Pahang : UMP, 2013Description: xviii, 39 p. : ill. ; 30 cm. + 1 CD-ROMISBN:

THE0002261(Local)

Subject(s):

Dissertation note: Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang – 2013 Abstract: Serine protease is widely used in many industrial applications especially in food industry because of their wide range of good solubility, substrate specificity, activity over wide pH and temperature range and high stability under extreme conditions. Benincasa hispida contains serine protease that usually can be found in the sarcocarp or seeds. Therefore, exocarp of Benincasa hispida is used determine the presence of serine protease. This research objective was to investigate the effect of pH, temperature and stability of the enzyme activities and also the enzyme kinetic of serine protease. Serine protease from exocarp of Benincasa hispida is purified using ammonium sulfate precipitation, and its activity at different parameters were measured by using ultraviolet-visible spectroscopy (uv-vis) at wavelength 660nm. The activity was inhibited by trichloroacetic acid, CCl3 COOH. The optimum pH for their activity is in alkaline range (pH7 – 9), and the enzyme activity dropped at pH11. Meanwhile, the optimum temperature of serine protease is in the range 50oC to 60oC, where its activity started to slows down at 70oC. The serine protease had a Michaelis-Menten constant, KM of 0.05172 mg/ml whereas the maximum rate of reaction, VMAX is . Serine protease activity is determined by the amount of enzyme that hydrolyzed casein to produce 1.0 µmole of tyrosine per minute.

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Holdings ( 2 )
Title notes ( 3 )

Holdings
Item type	Current library	Call number	Copy number	Status	Date due	Barcode
Final Year Report	UMPLIB GAMBANG	QP609.S47 S93 2013 rs Bc. (Browse shelf(Opens below))	1	Not for loan		0000074755
Final Year Report	UMPLIB GAMBANG	CD 7077 \| QP609.S47 S93 2013 rs Bc. (Browse shelf(Opens below))	1	Not for loan		0000074756

Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang – 2013

Bibliography : p. xix-xxii

Serine protease is widely used in many industrial applications especially in food industry because of their wide range of good solubility, substrate specificity, activity over wide pH and temperature range and high stability under extreme conditions. Benincasa hispida contains serine protease that usually can be found in the sarcocarp or seeds. Therefore, exocarp of Benincasa hispida is used determine the presence of serine protease. This research objective was to investigate the effect of pH, temperature and stability of the enzyme activities and also the enzyme kinetic of serine protease. Serine protease from exocarp of Benincasa hispida is purified using ammonium sulfate precipitation, and its activity at different parameters were measured by using ultraviolet-visible spectroscopy (uv-vis) at wavelength 660nm. The activity was inhibited by trichloroacetic acid, CCl3 COOH. The optimum pH for their activity is in alkaline range (pH7 – 9), and the enzyme activity dropped at pH11. Meanwhile, the optimum temperature of serine protease is in the range 50oC to 60oC, where its activity started to slows down at 70oC. The serine protease had a Michaelis-Menten constant, KM of 0.05172 mg/ml whereas the maximum rate of reaction, VMAX is . Serine protease activity is determined by the amount of enzyme that hydrolyzed casein to produce 1.0 µmole of tyrosine per minute.