Abstract:
:An extracellular endoglucanase (EG) that catalyzes the hydrolysis of carboxy-methyl cellulose (CMC) as substrate was purified to homogeneity from the soft-rot causing oomycete P. myriotylum with maximum EG production observed in presence of 1% (w/v) sucrose. The enzyme designated PmEG was observed to be monomeric with a molecular weight of 78 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Optimal activity of PmEG was determined at pH 5.0 and 25 °C with stability observed at pH extending over acidic to alkaline ranges viz., 3.0-10.0 and thermal stability upto 75 °C for 1 h. Optimal PmEG activity was obtained by addition of metal ions viz., Ca(2+) , Fe(3+) , Zn(2+) , Cu(2+) , Al(3+) , and also in presence of DTT and β-mercaptoethanol while it was inhibited by Cr(2+) . Various organic solvents, surfactants, and the oxidant, H2 O2 had little/no effect on PmEG activity reflecting its robustness and potential commercial significance. Kinetic constants of PmEG, Km and Vmax were determined as 1.1 mM and 407 µmol min(-1) mg(-1) protein, respectively. Glucose was observed to cause mixed non-competitive inhibition of PmEG.
journal_name
J Basic Microbioljournal_title
Journal of basic microbiologyauthors
Geethu C,Nair RAdoi
10.1002/jobm.201400323subject
Has Abstractpub_date
2014-12-01 00:00:00pages
1322-30issue
12eissn
0233-111Xissn
1521-4028journal_volume
54pub_type
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