| Purification and Characterization of Invertase Enzyme from Sugarcane (2004) | |||||
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Abstract | |||||
| Sugarcane invertase was purified from mature sugarcane stem tissue to an electrophoretically homogenous state, by successive ion-exchange chromatography on DEAE-Cellulose and CM-Cellulose column chromatography. The molecular weight of purified invertase enzyme was determined 218 kDa on SDS-Polyacrylamide slab gel electrophoresis. When the enzyme was characterized, it was found that the sugarcane invertase is glycoprotein in nature and it contained 7.29% sugar. The height enzyme activity was found at pH 7.2 and 60C temperature. The Km value of the enzyme was 8.0 mM. NaCl, MnCl2 increased invertase activity remarkably and KCl increased slightly while MgCl2, CaCl2 increased moderately. HgCl2 has completely and FeCl2 showed strong inhibitory effects on enzyme activity while EDTA and acetic acid have remarkable inhibitory effects on invertase activity. CuCl2, ZnCl2 and CdCl2 decreased invertase activity moderately. AgNO3, AlCl3, Glucose and Tris showed less inhibitory effects on invertase activity. | |||||
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