Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 68, Issue 2, Pages 168-173Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2010.10.006
Keywords
Peroxidase; Azide; Salicylic acid; Glycosylation
Funding
- Department of Biotechnology. Govt. of India, New Delhi
- Council of Scientific and Industrial Research, New Delhi
- U.P. Govt.
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Peroxidase was purified to homogeneity from a tree legume Leucaena leucocephala. On SDS-PAGE the purified enzyme exhibited two distinct subunits each of 66 and 58 kDa. Determination of native molecular weight of the purified peroxidase revealed a size of similar to 200 kDa suggesting a heterotrimeric structure (consisting of two subunits of 66 kDa and one subunit of 58 kDa) for native peroxidase. Purified peroxidase was found to be a glycoprotein (0.09 mg carbohydrates per mg purified peroxidase protein). Purified enzyme exhibited pH optimum of 5.0 and temperature optimum of 55 degrees C. The Michaelis-Menten constants (Km) for guaiacol, H2O2, were found to be 2.9 and 5.6 mM, respectively. Divalent cations namely, Ca2+ and Mn2+ activated peroxidase at lower concentration (up to 50 mM) while inhibited at higher concentration. Monovalent cation namely Na+ did not inhibit peroxidase at concentration as high as 4 M. L. leucocephala peroxidase was found to be unique as it was not inhibited by azide. (c) 2010 Elsevier B.V. All rights reserved.
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