Pectinesterase was extracted from potato alpha cultivar, purified and partially characterized The used protocol resulted in a 58.8-fold purification (51 850.2 units/mg protein) with 15.5% recovery of pectinesterase activity. The purified enzyme had a molecular weight of 27 kDa and its isoelectric point was around 4.5 with pH and temperature optima of 8.0 and 60°C, respectively. The purified enzyme had a single symmetric peak of specific activity after chromatographic steps. The homogeneity of the purified pectinesterase was confirmed by gel filtration and polyacrylamide electrophoresis gel
Authors wish to thank National Council for Science & Technology (CONACYT, México 83076/124550). This research was partially supported by the CGEPI-UAdeC and forms part of the thesis work of Julio Cesar Montañez. Authors wish to thank researchers of PP-4 of Biotechnology Dept, in the Universidad Autonoma Metropolitana Iztapalapa for facilities and critical opinions offered.
Peer reviewed