Kinetics of Peroxidase Production by <i>Streptomyces viridosporus</i> and Recombinant <i>Streptomyces lividans</i>

Korus, Roger A.; Lodha, Sanjay J; Adhi, Tri Partono; Crawford, Don L.

doi:10.1021/bp00012a005

Cited by 10 publications

(8 citation statements)

References 10 publications

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“…The peroxidase activity values for the highest yielding peroxidaseproducing strains in this study (0.228 U/ml for Streptomyces sp. MV28) were similar to those previously reported for peroxidases isolated from actinomycetes (Antonopoulous et al 2001;Korus et al 1991;Pasti et al 1990;Ramachandra et al 1987). Furthermore, the peroxidase activity was detected using 2,4-DCP as a substrate, which in a study by Pasti et al (1990), was shown to be a good substrate for assaying LiP produced by actinobacteria.…”

Section: Discussionsupporting

confidence: 89%

Actinobacteria isolated from termite guts as a source of novel oxidative enzymes

Roes‐Hill

Rohland

Burton

2011

Antonie van Leeuwenhoek

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A multi-faceted screening programme was designed to search for the oxidases, laccase, peroxidase and tyrosinase. Actinobacteria were selectively isolated from the paunch and colon region of the hindguts of the higher termite, Amitermes hastatus. The isolates were subjected to solid media assays (dye decolourization, melanin production and the utilization of indulin AT as sole carbon source) and liquid media assays. Eleven of the 39 strains had the ability to decolourize the dye RBBR, an indicator for the production of peroxidases in actinobacteria. Melanin production on ISP6 and ISP7 agar plates served as a good indicator for laccase and/or tyrosinase production and the ability of the strains to grow in the presence of indulin AT as a sole carbon source served as a good indicator of lignin peroxidase and/or general peroxidase production. Enzyme-producing strains were cultivated in liquid media and extracellular enzyme activities measured. Strains with the ability to produce oxidative enzymes under the conditions tested were identified to genus level by 16S rRNA gene analysis and compared to known oxidase producers. A strong relationship was observed between the environment sampled (termite guts where lignocellulose degradation occurs) and the dominant type of oxidative enzyme activity detected (laccases and peroxidases), which suggests the possibility of future targeted screening protocols linking the physical properties of the target enzymes with specific operational conditions required, such as lignocellulosic degradation in the preparation of biofuel feedstocks.

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Section: Discussionsupporting

confidence: 89%

Actinobacteria isolated from termite guts as a source of novel oxidative enzymes

Roes‐Hill

Rohland

Burton

2011

Antonie van Leeuwenhoek

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“…A number of genes including many heterologous ones have been cloned and expressed in Streptomyces species (Bender et al, 1990;Brawner, 1994;Erpicum et al, 1990;Fornwald et al, 1993;Illingworth et al, 1989;Korus et al, 1991) with the highest yields being reported for a heterologous gene (Binnie et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Fed-batch production ofThermomonospora fusca endoglucanase by recombinantStreptomyces lividans

Kim

Shin

Irwin

et al. 1998

Biotechnol. Bioeng.

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“…Four extracellular lignin peroxidase isoforms have been characterized and though all the isoforms require hydrogen peroxide as an electron donor, they differ in their substrate range (Ramachandra et al 1988). While P. chrysosporium secretes lignin peroxidase under nitrogen-, carbon-, or sulfurdeficient growth conditions (Kirk and Farrell 1987), S.viridosporus T7A was found to secrete lignin peroxidase during growth-associated conditions in nutrient-rich medium (Korus et al 1991). Another filamentous actinomycete, Streptomyces cyaneus CECT 3335, has been characterized and found to possess lignin-degrading abilities (Berrocal et al 2000).…”

Section: Lignin Degradation By Bacterial Secretionsmentioning

confidence: 99%

Lignocellulose Decomposition by Microbial Secretions

Santhanam

Badri

Decker

et al. 2011

Signaling and Communication in Plants

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Carbon storage in terrestrial ecosystems is contingent upon the natural resistance of plant cell wall polymers to rapid biological degradation. Nevertheless, certain microorganisms have evolved remarkable means to overcome this natural resistance. Lignocellulose decomposition by microorganisms comprises an essential step in closing the loop of the global carbon cycle as it facilitates the recycling of carbon reposited in the form of structural polymers in plant cell walls. The significance of microbial decomposition of lignocellulose has recently risen to greater heights with the revisitation of the potential of lignocellulosic biomass as a valuable and abundant feedstock for the renewable energy and bioproducts industry. The scope of this chapter is to succinctly touch upon the composition of lignocellulosic biomass, the major enzymes involved in decomposing lignocellulosic biomass, and the fungi and bacteria that secrete these enzymes.

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Kinetics of Peroxidase Production by Streptomyces viridosporus and Recombinant Streptomyces lividans

Cited by 10 publications

References 10 publications

Actinobacteria isolated from termite guts as a source of novel oxidative enzymes

Actinobacteria isolated from termite guts as a source of novel oxidative enzymes

Fed-batch production ofThermomonospora fusca endoglucanase by recombinantStreptomyces lividans

Lignocellulose Decomposition by Microbial Secretions

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