Enzyme–polysaccharide interaction: A method for improved stability of horseradish peroxidase

With the advent of green technology, use of enzymes as biocatalyst has become increasingly popular. However, in doing so, enzymes can lose their structure and catalytic activity under conditions that might be necessary for other components of processes. Compared to other strategies, chemical modification is a simple and effective technique for generating stable enzyme. Horseradish peroxidase (HRP; EC 1.11.1.7) was chemically modified by conjugating with 10 different polysaccharides. All polysaccharides were found to increase the thermal and pH stability of HRP with starch being most promising. Further, different parameters were evaluated for effective conjugation and thus stability of HRP conjugate. The degradation kinetics and storage stability of HRP proved the conjugate to be 6.4 times more stable than free enzyme. The starch conjugated HRP and free HRP were further evaluated for its application in decolorization of bromophenol blue dye. Both the enzymes were able to efficiently (>90%) decolorize the dye within minutes.