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090			_aB-6351
245	1	0	_aEffect of immobilization on pH and thermal stability of Aspergillus ficuum phytase
490	0		_vEnzyme and Microbial Technology, 25, p.517-521, 1999
520	3		_aThe phytase from Aspergillus ficuum catalyzes the hydrolysis of phytic acid into phosphoric acid and myo-inositol. The activity of this enzyme was determined by monitoring the rate of inositol production using high-performance liquid chromography methodology. The maximum activity of the enzyme was found to be approximately pH 5 and had a temperature optimum of 50°C. Under this condition, the kcat of 96 s-1 was obtained, and the corresponding Km for the catalysis of phytic acid was 2.34 mM. The optimum pH for the immobilized phytase was not much different from the intact enzyme. However, the optimum temperature was increased to 58°C, which is 8°C higher than that of free enzyme. Apparent Km for the immobilized enzyme was 3.28 mM, and only 34.6
650	1	4	_aASPERGILLUS FICUUM
650	1	4	_aPHYTASE
650	1	4	_aMYO-INOSITOL
700	1	2	_aLiu, B-L.
700	1	2	_aJong, C-H.
700	1	2	_aTzeng, Y.-M.
856	4	0	_uhttps://drive.google.com/file/d/1h_3-zyJx5bJNlWCIO-fXNkJ0IZxCdfd2/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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