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Journal ArticleDOI

Enhanced Expression and Hydrogen Peroxide Dependence of Lignin Peroxidase from Streptomyces viridosporus T7A

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TLDR
The volumetric and specific activities of Streptomyces viridosporus T7A lignin peroxidase isoform ALiP‐P3 were increased by formulating a novel corn‐starch‐based growth medium by optimizing the concentrations of starch, casein, yeast extract, CaCO3, NH4Cl, and trace metals.
Abstract
The volumetric and specific activities of Streptomyces viridosporus T7A lignin peroxidase isoform ALiP-P3 were increased by formulating a novel corn-starch-based growth medium by optimizing the concentrations of starch, casein, yeast extract, CaCO3 ,N H 4Cl, and trace metals. This medium increases cell densities by 10-fold, cell-specific ALiP-P3 activity by 6-fold, and volumetric ALiP-P3 activity by 60-fold compared to those obtained using a yeast-extract-based medium. The presence of increased concentrations of ALiP-P3 in the starch-based cultures was confirmed by Western blot analysis. In addition, the lignin peroxidase activity was found to be highly dependent upon the concentration of the necessary cofactor, hydrogen peroxide; using 2,4-dichlorophenol as the substrate, ALiP-P3 activity increased 1448-fold as the concentration of H2O2 was varied from 0.1 to 250 mM.

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Journal ArticleDOI

Biodegradation of diazo dye direct brown mr by acinetobacter calcoaceticus ncim 2890

TL;DR: Germination (%) and growth efficiency of Sorghum vulgare and Phaseolus mungo seeds revealed the degradation of DBMR into less toxic products than original dye, hence A. calcoaceticus can be applied for the commercial application.
BookDOI

Secretions and Exudates in Biological Systems

TL;DR: This volume brings together state-of-the-art information on the role of secretions and emissions in different organs and organisms ranging from flowers and roots of plants to nematodes and human organs.
Journal ArticleDOI

2,4-Dichlorophenol Degradation Using Streptomyces viridosporus T7A Lignin Peroxidase

TL;DR: The Streptomyces viridosporusT7A bacterium produces the extracellular lignin peroxidase ALiP‐P3, and the kinetics of the oxidation of 2,4‐dichlorophenol was examined to understand its kinetic behavior.
Journal ArticleDOI

Actinobacterial Peroxidases: an Unexplored Resource for Biocatalysis

TL;DR: This review article focuses on the different types of peroxidases found in actinobacteria, their natural role in these organisms and how they compare with the more well-described peroxids, and on work remaining to be done in this research field in order for per oxidases from actinOBacteria to be applied in industrial processes.
Journal ArticleDOI

Cloning of clustered Streptomyces viridosporus T7A lignocellulose catabolism genes encoding peroxidase and endoglucanase and their extracellular expression in Pichia pastoris.

TL;DR: In the best transformants, extracellular production of peroxidase by recombinant P. pastoris cultures was significantly higher than typically observed in S. viridosporus, and results indicate that lignocellulose catabolism genes may be clustered on the S. virginity chromosome.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

Enzymatic combustion: the microbial degradation of lignin

TL;DR: This paper presents a meta-analyses of IGNIN as a stimulus and its applications in medicine and physiology, and discusses the role that IGNIN plays in the development of disease and its role in medicine.
Journal ArticleDOI

Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase

TL;DR: An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography, finding that it is an oxygenase, unique in its requirement for H(2)O(2).
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