Abstract
Chitinases have been suggested to be involved in pathogen-antagonist interaction during biological control progress of plant pathogenic fungi. Here, a recombinant bacterial chitinase originally from Serratia marcescens B4A was produced, purified, and assayed biochemically to ascertain the activity and determine the kinetics parameters. Active enzyme was used to determine its biocontrol features against fungal phytopathogens. The results demonstrated that the optimum pH and temperature for the enzyme activity were 6.0 and 55 °C, respectively. The K(m) and V(max) values were 3.30 mg ml(-1) and 0.92 units, respectively. The recombinant chitinase was demonstrated to be highly active in controlling fungal pathogens.
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