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. 2013 Dec;36(12):1957-65.
doi: 10.1007/s00449-013-0972-9. Epub 2013 Jul 23.

Biochemical investigation of kraft lignin degradation by Pandoraea sp. B-6 isolated from bamboo slips

Affiliations

Biochemical investigation of kraft lignin degradation by Pandoraea sp. B-6 isolated from bamboo slips

Yan Shi et al. Bioprocess Biosyst Eng. 2013 Dec.

Abstract

Kraft lignin (KL) is the major pollutant in black liquor. The bacterial strain Pandoraea sp. B-6 was able to degrade KL without any co-substrate under high alkaline conditions. At least 38.2 % of chemical oxygen demand and 41.6 % of color were removed in 7 days at concentrations from 1 to 6 g L(-1). The optimum pH for KL degradation was 10 and the optimum temperature was 30 °C. The greatest activities of 2,249.2 U L(-1) for manganese peroxidase and 1,120.6 U L(-1) for laccase were detected on the third and fifth day at pH 10, respectively. Many small molecules, such as cinnamic acid, ferulic acid, 2-hydroxy benzyl alcohol, and vanillyl methyl ketone, were formed during the period of KL degradation based on GC-MS analysis. These results indicate that this strain has great potential for biotreatment of black liquor.

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Figures

Fig. 1
Fig. 1
Effect of temperature (a) and pH (b) on kraft lignin degradation by Pandoraea sp. B-6. Data are presented as mean of three replicates with SE
Fig. 2
Fig. 2
Pandoraea sp. B-6 growth and kraft lignin degradation. a Pandoraea sp. B-6 growth in different initial concentration, b kraft lignin removal rate by Pandoraea sp. B-6 on day 7 in different initial concentration, and c Pandoraea sp. B-6 growth and COD reduction in 2 g L−1 kraft lignin. Data are presented as mean of three replicates with SE
Fig. 3
Fig. 3
Color removal rate by Pandoraea sp. B-6 on day 7 in different initial concentrations of kraft lignin. Data are presented as mean of three replicates with SE
Fig. 4
Fig. 4
The activity of manganese peroxidase and laccase during the process of kraft lignin degradation by Pandoraea sp. B-6. a The activity of manganese peroxidase and laccase at different pH values on day 3. b The activity of manganese peroxidase and laccase during 7 days at pH 10. Cell-free supernatants were used as enzyme source for ligninolytic enzyme assays. Values are mean of three replicates with SE
Fig. 5
Fig. 5
The total ion chromatograph of trimethylsilyl derivatives of compounds extracted with trichloromethane from kraft lignin medium incubated with Pandoraea sp. B-6. a 0 days; b 3 days; and c 7 days

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