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Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine
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Jing-Han WANG1, Li PANG2, Hong TIAN1, Yi-Ya ZHAN1, Yong-Zhen YI1, Bo XIA1, *, Xia LIU1, *
Journal of Food Safety & Quality | 2025, 16(6) : 232 - 238
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Journal of Food Safety & Quality | 2025, 16(6): 232-238
• Special Topic: Application of Enzyme Technology in Food Engineering •
Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine
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Jing-Han WANG1, Li PANG2, Hong TIAN1, Yi-Ya ZHAN1, Yong-Zhen YI1, Bo XIA1, *, Xia LIU1, *
Affiliations
  • 1. College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China
  • 2. College of Horticulture, Hunan Agricultural University, Changsha 410128, China
Published: 2025-03-25 doi: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
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Objective To investigate the induced expression level and enzymatic properties of recombinant bacterial laccase and to improve the degradation efficiency of sulfadiazine antibiotics by bacterial laccase. Methods In this study, the effects of induction temperature, induction time, and concentration of isopropyl β-D-thiogalactopyranoside (IPTG) on enzyme expression were investigated by one-way experiments. The enzymatic properties of recombinant bacterial laccase were also investigated by both pH and temperature. Results The degradation of sulfadiazine by recombinant bacterial laccase at 24 h was 50%. The optimal conditions for the expression of recombinant bacterial laccase in Escherichia coli BL21 (DE3) were as follows: Induction temperature of 16 ℃, induction time of 16 h, and IPTG concentration of 0.2 mmol/L. The optimal pH was 3, and the stability was best at pH 7, with the enzyme activity reaching 150% in 6 h. The optimal temperature was 80 ℃, and the thermal stability was best at 70 ℃, with the enzyme activity increasing to 120% in 1 h. The half-life was about 6 h. Conclusion This study provides an experimental basis for the application of bacterial laccase in the degradation of sulfadiazine antibiotics and lays down a theoretical basis for the future study of its potential application in the industry.

bacterial laccase  /  sulfadiazine  /  antibiotic degradation  /  heterologous expression  /  enzymatic properties  /  protein concentration
Jing-Han WANG, Li PANG, Hong TIAN, Yi-Ya ZHAN, Yong-Zhen YI, Bo XIA, Xia LIU. Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine[J]. Journal of Food Safety & Quality, 2025 , 16 (6) : 232 -238 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
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Year 2025 volume 16 Issue 6
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Article Info
doi: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
  • Receive Date：2025-01-10
  • Online Date：2025-07-19
  • Published：2025-03-25
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  • Received：2025-01-10
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Affiliations
    1. College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China
    2. College of Horticulture, Hunan Agricultural University, Changsha 410128, China
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表12种不同金属材料的力学参数
科
Family		 属数
Number of
genus		 种数
Number of
species		 占总种数比例
Percentage of
total species (%)		 属
Genus		 种数
Number of
species		 占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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