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Journal article

Industrial dye decolorizing lignin peroxidase from Kocuria rosea MTCC 1532

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

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.

Language: English
Publisher: Springer-Verlag
Year: 2011
Pages: 217-223
ISSN: 18692044 and 15904261
Types: Journal article
DOI: 10.1007/s13213-011-0249-y
Keywords

Applied Microbiology Decolorization Dyes Fungus Genetics Life Sciences Lignin peroxidase Medical Microbiology Microbial Ecology Microbial Genetics and Genomics Microbiology Purification Zymogram

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