Characterisation of laccase produced by Coniothyrium minitans

JS Dahiya, D Singh, Poonam Singh - Nee Nigam

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A Coniothyrium minitans strain isolated from an experimental farm in Manitoba produced a substantial amount of an oxidoreductase enzyme, laccase in a 20 litre fermentation system using a simple production medium. This enzyme was purified to homogeneity by a simple procedure, the last stage of which involved hydrophobic interaction chromatography. Using this technique, over 120 mg of laccase protein was recovered per litre of fermented broth. The enzyme, with an estimated M-r of 74.000 and pI of 4.0, is a monomeric glycoprotein that contains 45% carbohydrate predominantly as mannose. It exhibited pH and temperature optima of 3.5 and 60 degrees C, respectively. Using 2,6-dimethoxyphenol as substrate the K-m value was found to be 100 mu M and the purified enzyme had a specific activity of 9.9 mkat per mg of protein.
LanguageEnglish
Pages349-359
JournalJOURNAL OF BASIC MICROBIOLOGY
Volume38
Issue number5-6
Publication statusPublished - 1998

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Coniothyrium minitans
laccase
enzymes
demonstration farms
Manitoba
oxidoreductases
mannose
glycoproteins
proteins
fermentation
carbohydrates
temperature

Cite this

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title = "Characterisation of laccase produced by Coniothyrium minitans",
abstract = "A Coniothyrium minitans strain isolated from an experimental farm in Manitoba produced a substantial amount of an oxidoreductase enzyme, laccase in a 20 litre fermentation system using a simple production medium. This enzyme was purified to homogeneity by a simple procedure, the last stage of which involved hydrophobic interaction chromatography. Using this technique, over 120 mg of laccase protein was recovered per litre of fermented broth. The enzyme, with an estimated M-r of 74.000 and pI of 4.0, is a monomeric glycoprotein that contains 45{\%} carbohydrate predominantly as mannose. It exhibited pH and temperature optima of 3.5 and 60 degrees C, respectively. Using 2,6-dimethoxyphenol as substrate the K-m value was found to be 100 mu M and the purified enzyme had a specific activity of 9.9 mkat per mg of protein.",
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Characterisation of laccase produced by Coniothyrium minitans. / Dahiya, JS; Singh, D; Singh - Nee Nigam, Poonam.

In: JOURNAL OF BASIC MICROBIOLOGY, Vol. 38, No. 5-6, 1998, p. 349-359.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterisation of laccase produced by Coniothyrium minitans

AU - Dahiya, JS

AU - Singh, D

AU - Singh - Nee Nigam, Poonam

PY - 1998

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AB - A Coniothyrium minitans strain isolated from an experimental farm in Manitoba produced a substantial amount of an oxidoreductase enzyme, laccase in a 20 litre fermentation system using a simple production medium. This enzyme was purified to homogeneity by a simple procedure, the last stage of which involved hydrophobic interaction chromatography. Using this technique, over 120 mg of laccase protein was recovered per litre of fermented broth. The enzyme, with an estimated M-r of 74.000 and pI of 4.0, is a monomeric glycoprotein that contains 45% carbohydrate predominantly as mannose. It exhibited pH and temperature optima of 3.5 and 60 degrees C, respectively. Using 2,6-dimethoxyphenol as substrate the K-m value was found to be 100 mu M and the purified enzyme had a specific activity of 9.9 mkat per mg of protein.

M3 - Article

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