Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Abstract

Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from Aspergillus niger KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.

Operational Stability, Regenerability, and Thermodynamics Studies on Biogenic Silica/Magnetite/Graphene Oxide Nanocomposite-Activated Candida rugosa Lipase

“…The study findings were consistent with the following results published in the following literature. Bodakowska-Boczniewicz and Garncarek [45] observed a similar outcome on the E a of free Naringinase (25.18 kJ/mol) in comparison to its immobilized form on magnetic polysaccharide support (17.66 kJ/mol). In another study, Liu et al [46] similarly reported higher E a for free Burkholderia cepacia lipase (25.18 kJ/mol) than the immobilized form (17.66 kJ/mol).…”

Recent Strategies and Applications for l-Asparaginase Confinement

“…Among the described works, maltose-functionalised magnetic core/shell Fe 3 O 4 @Au NPs [ 74 ] seem to be the most promising nanomaterial for ASNase confinement by physical adsorption due to the highest η i displayed (77.2%), along with the high TS (90% of activity after 3 h of incubation at 55 °C) and SS (64% of activity following 28 days at 25 °C), ability to keep half of its initial enzymatic activity after 13 cycles of reaction (OS) and enhanced confined ASNase affinity. The combination of (nano)materials with magnetic properties allows for an easy separation process [ 22 , 110 , 111 ], providing a good option for the ASNase confinement.…”

“…Thus, the improvement of ASNase enzymatic and therapeutic properties has been achieved by introducing chemical modifications and physical integration within several supports. These techniques, if properly designed, can improve the enzymes stability and allow their reuse, also contributing to the reduction of operation costs [ 21 , 22 , 23 , 24 ]. Due to enzymes protection (enhanced activity and stability [ 25 , 26 ]) and expanded catalytic half-life [ 27 ], confined ASNase can find improved applications in a wide range of areas, namely as sustained or continuous-release delivery systems, as biosensors in clinical diagnosis, as biocatalysts in the food industry, among other [ 24 ].…”

Novel Strategy of Mussel-Inspired Immobilization of Naringinase with High Activity Using a Polyethylenimine/Dopamine Co-deposition Method

“…Huang et al 10 successfully immobilized naringinase in electrospun cellulose acetate nanofibers using a layer-by-layer self-assembly technique, and the final enzyme activity reached 0.122 U/g. Bodakowska-Boczniewicz et al 11 immobilized naringinase on a magnetic carrier activated by polyethylenimine (PEI), and 16.40 U/g of enzyme activity was obtained. It could be seen that the enzyme activity was still very low in the present works.…”