What is it about?

Polygalacturonase isoenzyme 3 (PG-3) was purified to homogeneity with a specific activity of 0.7 μ katal mg−1 protein from banana fruit pulp. The purified enzyme was characterized as a glycoprotein with ca. 8% carbohydrate, and the molecular weight of the native enzyme to be 90 ± 10 kDa with a subunit molecular weight of 29 ± 2 kDa.

Featured Image

Why is it important?

As a unique property of the enzyme was the requirement of –SH groups for the enzyme activity. The enzyme was inhibited by p-CMB and activated by 2-ME and DTT. The inhibition of p-CMB could be reversed by DTT. The enzyme contained eight free –SH groups. The Km of the enzyme was 0.15% for polygalacturonic acid.

Perspectives

The study provides new insights into propagating further studies in view of developing certain synthetic inhibitors probably playing role in delaying of banana as well as similar types of fruits.

SANJAY MISHRA

Read the Original

This page is a summary of: Purification and characterization of polygalacturonase from banana fruit, Phytochemistry, May 2000, Elsevier,
DOI: 10.1016/s0031-9422(00)00061-3.
You can read the full text:

Read

Contributors

The following have contributed to this page