Cassava pullulanase and its synergistic debranching action with isoamylase 3 in starch catabolism.

ABSTRACT: Pullulanase (EC 3.2.1.41, PUL), a debranching enzyme belonging to glycoside hydrolase family 13 subfamily 13, catalyses the cleavage of α-1,6 linkages of pullulan and β-limit dextrin. The present work studied PUL from cassava Manihot esculenta Crantz (MePUL) tubers, an important economic crop. The Mepul gene was successfully cloned and expressed in E. coli and rMePUL was biochemically characterised. MePUL was present as monomer and homodimer, as judged by apparent mass of ~ 84 - 197 kDa by gel permeation chromatography analysis. Optimal pH and temperature were at pH 6.0 and 50 °C, and enzyme activity was enhanced by the addition of Ca²⁺ ions. Pullulan is the most favourable substrate for rMePUL, followed by β-limit dextrin. Additi

SUBMITTER: Wangpaiboon K 

PROVIDER: S-EPMC9911869 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature