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Armoracia rusticana is the commercial source of the enzyme Horseradish Peroxidase (HRP). Calcium ions play an important role in the functional conformation of HRP. The present study assesses the effect of three calcium salts viz., calcium chloride (CaCl 2 ), calcium nitrate [Ca(NO 3 ) 2 ] and calcium sulphate (CaSO 4 ) on the guaiacol activity of crude peroxidase extracted from the shoots and roots of in vitro grown plantlets of A. rusticana and their growth medium. The highest activity was observed in the shoot extracts of 25 mM CaCl 2 treated plantlets (1.92 U/mL) and the root extracts of 25 mM Ca(NO 3 ) 2 supplemented plantlets (2.84 U/mL). The crude peroxidase activity of the medium containing 25 mM CaCl 2 supplement was highest (0.13 U/mL). The capacity of the shoot and root extracts to decolourise a 10 ppm solution of methyl orange over 48 hours, was also tested. The decolourisation capacity was highest in the shoot extracts from CaCl 2 treated plantlets (49.32%) and root extracts from Ca(NO 3 ) 2 treated plantlets (29.72%) respectively. Hence, the addition of calcium salts to growth medium enhances both peroxidase activity and decolourisation capacity of crude extracts of A. rusticana plantlets. These findings are of significance in enzymatic treatment for decolourisation of effluents containing dyestuffs.

The decolourisation of Methyl Orange (MO) and Bismarck Brown (BB) by crude peroxidase from Armoracia rusticana (Horseradish) was studied by varying different reaction parameters. The pH of the reaction mixture, initial dye concentration, amount of enzyme and hydrogen peroxide concentration were optimised for ambient temperatures (30 ± 2°C). The optimum pH for decolourisation was 4.0 (72.95 %) and 3.0 (79.24 %) for MO and BB, respectively. Also it was found that the Chemical Oxygen Demand of the enzyme-treated sample was significantly lower than that of the untreated controls for both dyes. The addition of a complex iron salt like Ferric EDTA was found to enhance the decolourisation of both dyes at pH 6.0, showing an increase of 8.69 % and 14.17 % in the decolourisation of MO and of BB, respectively. The present study explores the potential of crude peroxidase from horseradish to decolourise representative monoazo and diazo dyes, MO and BB, respectively. An attempt has been made to utilise a crude enzyme with appreciable activity obtained after minimal processing for the decolourisation of the aforesaid dyes. The findings of this study would find application in the enzymatic treatment of wastewater containing azo dyes.

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