Efficient immobilization of agarase using carboxyl-functionalized magnetic nanoparticles as support
Electron. j. biotechnol
;
25: 13-20, ene. 2017. ilus, graf
Article
in English
| LILACS
| ID: biblio-1008291
ABSTRACT
Background:
A simple and efficient strategy for agarase immobilization was developed with carboxyl-functionalized magnetic nanoparticles (CMNPs) as support. The CMNPs and immobilized agarase (agarase-CMNPs) were characterized by transmission electron microscopy, dynamic light scattering, vibrating sample magnetometry, scanning electron microscopy, X-ray diffraction, thermogravimetric analysis, and zeta-potential analysis. The hydrolyzed products were separated and detected by ESI-TOF-MS.Results:
The agarase-CMNPs exhibited a regular spherical shape with a mean diameter of 12 nm, whereas their average size in the aqueous solution was 43.7 nm as measured by dynamic light scattering. These results indicated that agarase-CMNPs had water swelling properties. Saturation magnetizations were 44 and 29 emu/g for the carriers and agarase-CMNPs, respectively. Thus, the particles had superparamagnetic characteristics, and agarase was successfully immobilized onto the supports. Agaro-oligosaccharides were prepared with agar as substrate using agarase-CMNPs as biocatalyst. The catalytic activity of agarase-CMNPs was unchanged after six reuses. The ESI-TOF mass spectrogram showed that the major products hydrolyzed by agarase-CMNPs after six recycle uses were neoagarotetraose, neoagarohexaose, and neoagarooctaose. Meanwhile, the end-products after 90 min of enzymatic treatment by agarase-CMNPs were neoagarobiose and neoagarotetraose.Conclusions:
The enhanced agarase properties upon immobilization suggested that CMNPs can be effective carriers for agarase immobilization. Agarase-CMNPs can be remarkably used in developing systems for repeated batch production of agar-derived oligosaccharides.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Oligosaccharides
/
Enzymes, Immobilized
/
Magnetite Nanoparticles
/
Glycoside Hydrolases
Language:
English
Journal:
Electron. j. biotechnol
Journal subject:
Biotechnology
Year:
2017
Type:
Article
/
Project document
Affiliation country:
China
Institution/Affiliation country:
Jimei University/CN
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