Open AccessPreparation of immobilized arylsulfatase on magnetic Fe 3 O 4 nanoparticles and its application for agar quality improvement
Author(s) -
Zhang Chenghao,
Jiang Zedong,
Li Hebin,
Ni Hui,
Zheng Mingjing,
Li Qingbiao,
Zhu Yanbing
Publication year - 2021
Publication title -
food science and nutrition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 27
ISSN - 2048-7177
DOI - 10.1002/fsn3.2446
Subject(s) - agar , fourier transform infrared spectroscopy , thermal stability , immobilized enzyme , arylsulfatase , chemistry , nuclear chemistry , arylsulfatase a , hydrolysis , chromatography , magnetic nanoparticles , materials science , nanoparticle , chemical engineering , biochemistry , enzyme , organic chemistry , nanotechnology , biology , genetics , bacteria , engineering
Abstract 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 Fe 3 O 4 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 K m and V max 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.