Characterization of xerophytic thermophilic laccase exhibiting metal ion-dependent dye decolorization potential

Applied Biochemistry and Biotechnology
Gali Nirmal Kumar, Kotteazeth Srikumar

Abstract

Five laccase enzyme isoforms were isolated and purified to homogeneity from the cladodes of xerophytic Cereus pterogonus and Opuntia vulgaris plant species. Catalytic activity of all isoforms was enhanced 40 % by 1 mM Cu(2+) and 1 mM Mn(2+), whereas the activity was inhibited 100 % by 10 mM Fe(2+). Enzyme was found stable in 4 M urea and exhibited inactivity of 50 % in 8 M urea concentration. Ethylenediaminetetraacetic acid and cysteine-HCl were able to completely inhibit the enzyme activity at 1 mM and 100 μM, respectively. Preheated enzyme samples showed enhanced and stable catalytic activity in the presence of divalent cations over a period of 30 min compared with controls. In the presence of metal ions (1 mM Cu(2+) and 1 mM Mn(2+)), the preheated enzyme forms (60-90 °C) achieved 97 % of Malachite green and 98.75 % of Indigo blue (both at 2 %, w/v) dye decolorization in 12 h.

References

May 8, 2004·Aquatic Toxicology·Shivaji SrivastavaD Roy
Jul 7, 2005·Extremophiles : Life Under Extreme Conditions·Kentaro Miyazaki
Sep 23, 2008·Journal of Hazardous Materials·B H Hameed, T W Lee
Oct 22, 2008·Applied Biochemistry and Biotechnology·Said GalaiM Nejib Marzouki
Apr 10, 2009·Journal of Hazardous Materials·Kumarasamy MurugesanYoon-Seok Chang
Sep 3, 2010·Biomedical Chromatography : BMC·Gali Nirmal Kumar, Kotteazeth Srikumar

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Citations

Nov 13, 2013·Applied Biochemistry and Biotechnology·Gali Nirmal Kumar, Kotteazeth Srikumar
Feb 2, 2018·Critical Reviews in Biotechnology·Aysha Hamad AlneyadiS Salman Ashraf
May 28, 2013·Journal of Environmental Science and Health. Part A, Toxic/hazardous Substances & Environmental Engineering·Kana InoueKitao Fujiwara

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