This study aimed to improve the catalytic ability of Thermobifida fusca dye-decolorizing peroxidase (TfuDyP) to degrade anthraquinone dyes. The recombinant plasmid pET-28a(+)-TfuDyP was transformed into Escherichia coli BL 21 for heterologous expression, and the fermentation conditions of recombinant TfuDyP was optimized. Additionally, the relationship between enzyme activity and heme saturation was analyzed. SDS-PAGE showed that the molecular weight of recombinant TfuDyP was 46 kDa. Moreover, induction with 0.3 mmol/L IPTG at 30 ℃ for 14 h was determined to be the optimal fermentation condition. Under this condition, the specific activity of TfuDyP was 27.9 U/g. Furthermore, hemin, 5-aminolevulinic acid (5-ALA), glutamic acid (Glu), FeCl2 and MnCl2 promoted the enzyme activity. There was a positive correlation between the increase in enzyme activity and heme saturation. Therefore, this study provides a theoretical basis for improving heme saturation by adding exogenous promoters and applying this in industrial fermentation of dye-decolorizing peroxidase.
ZHU Zhubing
,
SUN Yawu
,
TANG Lei
. Expression and fermentation optimization of dye-decolorizing peroxidase from Thermobifida fusca[J]. Food and Fermentation Industries, 2019
, 45(13)
: 23
-30
.
DOI: 10.13995/j.cnki.11-1802/ts.019526
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