Chitinase: purification and characterization from Alternaria brassicicola and its antibacterial activity.
TL;DR
A newly characterized extracellular chitinase enzyme was purified from Alternaria brassicicola using methods including ammonium sulfate precipitation and gel filtration chromatography and demonstrates inhibitory activity against bacteria such as Staphylococcus aureus and Escherichia coli.
Abstract
Chitinases, a class of enzymes found widely in organisms such as bacteria, yeasts, fungi, arthropods, actinomycetes, plants and humans, exhibit significant diversity in their molecular structure, catalytic mechanisms and substrate preferences. A newly characterized extracellular chitinase enzyme was purified from Alternaria brassicicola using methods including ammonium sulfate precipitation and gel filtration chromatography. The enzyme's molecular weight, determined via SDS-PAGE, was found to be 44 kDa. It displays optimal activity at a temperature of 35 °C and remains functional across a temperature range of 30-60 °C. The enzyme exhibits maximum activity at pH 6.6 and shows significant activity within a pH range of 4-8. Metal ion studies revealed that Cu2+, Ca2+ and Zn2+ inhibits its activity, while Mn2+ and Mg2+ enhances it. Furthermore, the enzyme demonstrates inhibitory activity against bacteria such as Staphylococcus aureus and Escherichia coli. These findings underscore its potential applications in various biotechnological and medical fields.