Purification and molecular properties of papaya pectinesterase

• Main Authors: Fayyaz, A., Asbi, B.A., Ghazali, H.M., Che Man, Y.B., Jinap, S.
• Format: Article
• Language: English
• Published: Elsevier 1994
• Online Access: http://psasir.upm.edu.my/id/eprint/113113/1/113113.pdf; http://psasir.upm.edu.my/id/eprint/113113/; https://linkinghub.elsevier.com/retrieve/pii/0308814694900078
• Institution: Universiti Putra Malaysia

Pectinesterase (EC 3.1.1.11) was extracted and purified from papaya (Carica papaya L. var. exotica). The procedure adopted for purification resulted in an approximate 250-fold purification (784 units/mg protein) with a 45% recovery of the pectinesterase activity. The enzyme was eluted in a single peak after CmdashSephadex and Sephadex G-100 chromatography. The purified enzyme had a uniform specific activity throughout the final chromatographic peak. The enzyme preparation was confirmed to be of homogeneous state by gel filtration and nondashdenaturing polyacrylamide gel electrophoresis and it has a molecular weight of approximately 32 000 Da.