Industrial dye decolorizing lignin peroxidase from Kocuria rosea MTCC 1532

Ganesh Kashinath Parshetti, Supriya Parshetti, Dayanand Kalyani, Ruey-an Doong, Sanjay P. Govindwar

Research output: Contribution to journalJournal articleResearchpeer-review


Lignin peroxidase (LiP) enzyme was purified from Kocuria rosea MTCC 1532. The enzyme was produced and subjected to purification by ion exchange chromatography followed by gel filtration chromatography; 79-fold purity was obtained. The molecular weight of LiP was determined to be 66 kDa. The pH optimum of the purified enzyme was 3.0, and the temperature optimum was found to be around 50°C. Purified LiP showed a much higher activity towards n-propanol than towards L-Dopa, 8-hydroquinone, mimosine, veratryl alcohol, and xylidine. The effect of inhibitor and metal ion on LiP activity was analyzed. Purified LiP was able to decolorize synthetic dyes from various groups, indicating that it is a versatile peroxidase.
Original languageEnglish
JournalAnnals of Microbiology
Issue number1
Pages (from-to)217-223
Publication statusPublished - 2012
Externally publishedYes


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