Siti Syarrah Mohammad Hanapiah creator text theses my Kuantan, Pahang UMP 2013 monographic eng

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xviii, 39 p. : ill. ; 30 cm. + 1 CD-ROM 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. specialized Siti Syarrah Mohammad Hanapiah Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang – 2013 Bibliography : p. xix-xxii Serine proteinases Cucurbitaceae THE0002261(Local) UMP 131113 20251114204546.0 vtls000076087