sc9b05796_si_001.pdf (2.73 MB)

Tyrosinase-Catalyzed Phenol-Mediated Immobilization of β‑Agarase on l‑Lysine-Coated Magnetic Particles for the Production of Neoagarooligosaccharides from Gelidium amansii

Download (2.73 MB)
journal contribution
posted on 27.02.2020, 19:50 by Teklebrahan Gebrekrstos Weldemhret, Grace Masbate Nisola, Kristine Rose Medina Ramos, Angelo Bautista Bañares, Kris Niño Gomez Valdehuesa, Won-Keun Lee, Wook-Jin Chung
Cross-linked enzyme aggregates of β-agarase (Aga2) were immobilized on l-lysine-coated magnetic nanoparticles (Lys@Fe3O4) for the production of neoagarooligosaccharides (NAOSs) from Gelidium amansii. The support Lys@Fe3O4 was prepared in a one-pot aqueous medium, whereas Aga2 was engineered to carry five tyrosine residues at its N-terminus (Aga2Y5N). Cross-linked immobilization of Aga2Y5N on Lys@Fe3O4 was effectively catalyzed by tyrosinase but its efficiency was further improved with phenol addition, affording the best biocatalyst, Aga2Y5N-TP@Lys@Fe3O4. Although its kinetic properties were slightly reduced, the overall results show that Aga2Y5N-TP@Lys@Fe3O4 performed remarkably better than free Aga2Y5N, as reflected by its excellent stability at wider pH and temperature ranges. Moreover, Aga2Y5N-TP@Lys@Fe3O4 can be effectively collected and recycled through magnetization, unlike the free Aga2Y5N, which cannot be easily retrieved from the reaction mixture after use. Hydrolysis results demonstrate the capability of Aga2Y5N-TP@Lys@Fe3O4 to effectively and selectively produce NAOS as a mixture of neoagarotetraose and -hexaose. The proposed route could be useful for the immobilization of other enzymes in various biotechnological applications.

History

Exports