Elicitation of lignin peroxidase inStreptomyces lividans

Yee, Dennis C.; Wood, Thomas K.

doi:10.1007/bf02788068

Cited by 5 publications

(2 citation statements)

References 21 publications

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“…Organism and Culture Conditions. S. viridosporus T7A (ATCC 39115) was supplied by Prof D. L. Crawford (University of Idaho, Moscow, ID) and cultivated at 30 °C in 50 mL of starch‐containing DJMM, as described previously (Yee and Wood, 1996). The cultures were harvested for ALiP‐P3 after 6 days, as described below.…”

Section: Methodsmentioning

confidence: 99%

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

Yee

Wood

1997

Biotechnol. Prog.

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The Streptomyces viridosporus T7A bacterium produces the extracellular lignin peroxidase ALiP-P3. The ALiP-P3-catalyzed oxidation of 2,4-dichlorophenol (DCP) was examined to understand its kinetic behavior. Initial rate data of the oxidation of DCP were obtained by a spectrophotometric peroxidase assay, and the kinetics were best modeled with a random-binding bireactant system, which differs from the ping-pong bireactant system that is typically used for horseradish peroxidase and lignin peroxidase from the fungus Phanerochaete chrysosporium, and suggests that either DCP or H2O2 may bind first to ALiP-P3. Chloride ion measurements indicate that 16% of the reacted DCP was fully dechlorinated by ALiP-P3. Chemical ionization mass spectrometry was also utilized to identify the DCP degradation product as a hydrophobic chlorinated dimer of mass 322.

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Section: Methodsmentioning

confidence: 99%

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

Yee

Wood

1997

Biotechnol. Prog.

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“…Peroxidase activity was assayed by using 2,4-dichlorophenol (2,4-DCP) (Sigma-Aldrich, Stockholm, Sweden) as the substrate. The reaction mixture (1 mL) contained 100 mM sodium acetate buffer (pH 5.5), 82 mM 4-aminoantipyrine (Sigma-Aldrich, Stockholm, Sweden), 20 mM 2,4-DCP, 40 mM hydrogen peroxide, and an appropriate amount of LsLiP (Yee and Wood 1996). The reaction was initiated by the addition of hydrogen peroxide, during the first 2 min of the reaction at 35 °C at 510 nm.…”

Section: Enzyme Activity Assaymentioning

confidence: 99%

Lignin peroxidase from the white-rot fungus Lentinus squarrosulus MPN12 and its application in the biodegradation of synthetic dyes and lignin

Giáp

Nghị

Cuong

et al. 2022

BioRes

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Lignin peroxidase (LiP), which has been studied extensively in white-rot basidiomycetes and their potential to degrade dyes from textile wastewater, plays a role in the biodegradation of lignin from pulp and paper industry wastewater, as well as agricultural waste. Lignin peroxidase (LsLiP) was successfully purified from the newly isolated Lentinus squarrosulus MPN12 with a 47.1-fold purification and a 15.7% yield. After 48 h-incubation, LsLiP was able to decolorize all tested dyes up to 92% for Acid Blue 62 (NY3), followed by Porocion Brilliant blue HGR (PB, 73.5%), Acid Blue 281 (NY5, 70.5%), Acid Blue 113 (IN13, 61%), Acid red 266 (NY7, 56%), and 34.5% for Acid red 299 (NY1), compared to the negative control with the heat-denatured enzyme. The biodegradation potential of LsLiP was further suggested by the change of lignin structure based on Fourier transform infrared (FTIR) analyses. Lignin structure was noticeably changed before and after LsLiP treatment, especially in the fingerprint regions (1600 to 1000 cm-1) and 2930 cm-1 corresponding to the stretching vibrations of various groups in lignin. Thus, LsLiP has potential application in both enzyme-based decolorization of synthetic dyes and lignin biodegradation.

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One stop mycology

Frazer

1997

Mycological Research

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Elicitation of lignin peroxidase inStreptomyces lividans

Cited by 5 publications

References 21 publications

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

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

Lignin peroxidase from the white-rot fungus Lentinus squarrosulus MPN12 and its application in the biodegradation of synthetic dyes and lignin

One stop mycology

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