Zhang Chenghao, Jiang Zedong, Li Hebin, Ni Hui, Zheng Mingjing, Li Qingbiao, Zhu Yanbing
College of Food and Biological Engineering Jimei University Xiamen China.
Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering Xiamen China.
Food Sci Nutr. 2021 Jul 7;9(9):4952-4962. doi: 10.1002/fsn3.2446. eCollection 2021 Sep.
The presence of sulfate groups in agar compromises the agar quality by affecting the crosslinking during gelling process. Some arylsulfatases can catalyze the hydrolysis of sulfate bonds in agar to improve the agar quality. Immobilized arylsulfatases prove beneficial advantages for their industrial applications. Here, a previously characterized mutant arylsulfatase K253H/H260L was immobilized on the synthesized magnetic FeO nanoparticles after functionalization by tannic acid (MNPs@TA). The surface properties and molecular structures of the immobilized arylsulfatase (MNPs@TA@ARS) were examined by scanning electron microscopy and Fourier transform infrared spectroscopy. Enzymatic characterization showed that MNPs@TA@ARS exhibited shifted optimal temperature and pH with deviated apparent and compared to its free counterpart. The immobilized arylsulfatase demonstrated improved thermal and pH stability and enhanced storage stability with modest reusability. In addition, MNPs@TA@ARS displayed enhanced tolerance to various inhibitors and detergents. The utilization of the immobilized arylsulfatase for agar desulfation brought the treated agar with improved quality.
琼脂中硫酸根的存在会在凝胶过程中影响交联,从而损害琼脂质量。一些芳基硫酸酯酶可以催化琼脂中硫酸键的水解,以提高琼脂质量。固定化芳基硫酸酯酶在其工业应用中显示出有益的优势。在此,先前表征的突变型芳基硫酸酯酶K253H/H260L在经单宁酸功能化后的合成磁性FeO纳米颗粒(MNPs@TA)上进行了固定化。通过扫描电子显微镜和傅里叶变换红外光谱对固定化芳基硫酸酯酶(MNPs@TA@ARS)的表面性质和分子结构进行了检测。酶学表征表明,与游离的对应物相比,MNPs@TA@ARS表现出最佳温度和pH的偏移,表观 和 也有所偏差。固定化芳基硫酸酯酶表现出改善的热稳定性和pH稳定性,以及增强的储存稳定性和适度的可重复使用性。此外,MNPs@TA@ARS对各种抑制剂和去污剂表现出增强的耐受性。利用固定化芳基硫酸酯酶进行琼脂脱硫可使处理后的琼脂质量得到改善。