Optimization of κ-Selenocarrageenase Production by <i>Pseudoalteromonas sp</i>. Xi13 and Its Immobilization
Yashan Deng,
Xixi Wang,
Hui Xu,
Cui Liu,
Ran Li,
Yuanyuan Zhang,
Changfeng Qu,
Jinlai Miao
Affiliations
Yashan Deng
Department of Pharmaceutical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Xixi Wang
Key Laboratory of Marine Eco-Environmental Science and Technology, First Institute of Oceanography, Ministry of Natural Resources, Qingdao 266061, China
Hui Xu
Department of Pharmaceutical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Cui Liu
Department of Pharmaceutical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Ran Li
Department of Pharmaceutical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Yuanyuan Zhang
Department of Pharmaceutical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Changfeng Qu
Key Laboratory of Marine Eco-Environmental Science and Technology, First Institute of Oceanography, Ministry of Natural Resources, Qingdao 266061, China
Jinlai Miao
Key Laboratory of Marine Eco-Environmental Science and Technology, First Institute of Oceanography, Ministry of Natural Resources, Qingdao 266061, China
The bioenzymatic production of selenium oligosaccharides addresses the problems resulting from high molecular weight and poor water solubility of κ-selenocarrageenan, and lays foundation for its application as adjuvant drugs for cancer treatment and food additive. κ-selenocarrageenase extracted from Pseudoalteromonas sp. Xi13 can degrade κ-selenocarrageenan to selenium oligosaccharides. The maximum optimized κ-selenocarrageenase activity using Response Surface Methodology (RSM) was increased by 1.4 times, reaching 8.416 U/mL. To expand applications of the κ-selenocarrageenase in industry, the preparation conditions of it in either lyophilized or immobilized form were investigated. The activity recovery rate of the lyophilized enzyme was >70%, while that of the immobilized enzyme was 62.83%. However, the immobilized κ-selenocarrageenase exhibits good stability after being reused four times, with 58.28% of residual activity. The selenium content of κ-selenocarrageenan oligosaccharides degraded by the immobilized κ-selenocarrageenase was 47.06 µg/g, 8.3% higher than that degraded by the lyophilized enzyme. The results indicate that the immobilized κ-selenocarrageenase is suitable for industrial applications and has commercial potential.
