Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization.
Optimization of κ-Selenocarrageenase Production by Pseudoalteromonas sp. Xi13 and Its Immobilization.
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DOI：
10.3390/molecules27227716
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发表时间：
2022-11-09
期刊：
影响因子：
--
通讯作者：
Miao J
中科院分区：
文献类型：
--
作者：
Deng Y;Wang X;Xu H;Liu C;Li R;Zhang Y;Qu C;Miao J
生物酶法生产硒寡糖，解决了κ-硒卡拉胶分子量大、水溶性差的问题，为其作为抗癌辅助药物和食品添加剂的应用奠定了基础。从假交替单胞菌（Pseudoalteromonassp.Xi13）中提取的κ-硒化卡拉胶酶可将κ-硒化卡拉胶降解为硒寡糖。响应面法优化后的最大酶活为8.416 U/mL，比优化前提高了1.4倍。为扩大κ-硒化卡拉胶酶在工业上的应用，研究了κ-硒化卡拉胶酶的冻干和固定化制备条件。冻干酶活力回收率大于70%，固定化酶活力回收率为62.83%。固定化κ-硒化卡拉胶酶重复使用4次后仍保持58.28%的活力，稳定性良好。固定化κ-硒化卡拉胶酶降解的κ-硒化卡拉胶寡糖含硒量为47.06 μg/g，比冻干酶高8.3%。结果表明，固定化κ-硒化卡拉胶酶具有良好的工业应用前景。
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.
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