Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Abstract

Naringinase is an enzyme complex which exhibits α-l-rhamnosidase and β-d-glucosidase activity. This enzymatic complex catalyzes the hydrolysis of naringin (4′,5,7-trihydroxy flavanone 7-rhamnoglucoside), the main bittering component in grapefruit. Reduction of the level of this substance during the processing of juice has been the focus of many studies. The aim of the study was the immobilization of naringinase on chitosan microspheres activated with glutaraldehyde and, finally, the use of such immobilized enzyme for debittering grapefruit juice. The effect of naringinase concentration and characterization of the immobilized enzyme compared to the soluble enzyme were investigated. The maximum activity was observed at optimum pH 4.0 for both free and immobilized naringinase. However, the optimum temperature was shifted from 70 to 40 °C upon immobilization. The KM value of the immobilized naringinase was higher than that of soluble naringinase. The immobilization did not change the thermal stability of the enzyme. The immobilized naringinase had good operational stability. This preparation retained 88.1 ± 2.8% of its initial activity after ten runs of naringin hydrolysis from fresh grapefruit juice. The results indicate that naringinase immobilized on chitosan has potential applicability for debittering and improving the sensory properties of grapefruit juices.

Chitosan-Grafted Halloysite Nanotubes-Fe3O4 Composite for Laccase-Immobilization and Sulfamethoxazole-Degradation

“…This may be due to the saturation of sites on the HNTs-M-chitosan (1%)-GTA available for immobilization. A similar effect was observed for the loading of the enzyme naringinase on chitosan microspheres [ 41 ]. The thermal stability is shown in Figure 7 B.…”

Editorial for Special Issue: Enzyme Immobilization and Its Applications

“…Immobilization of other enzymes is also treated in this Special Issue. Naranginase (presenting both α-l-rhamnosidase and β-d-glucosidase activities) was immobilized on chitosan particles activated with glutaraldehyde and utilized in the debittering of grapefruit [34]. A carbon screen-printed platform made from ceramic substrate was coated with poly(3,4-ethylenedioxythiophene)/poly(styrenesulfonate) to immobilize acetylcholinesterase and used to quantify acetylcholine [35].…”

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

“…There are only a few articles on the immobilization of naringinase on magnetic carriers in the literature [ 16 , 37 , 38 , 39 ], including one on a magnetic polysaccharide carrier [ 21 ]. However, most of these studies lack information on the thermodynamic characteristics of the immobilized enzyme.…”

“…Polysaccharide carriers, thanks to the presence of many chemically active groups, relatively large specific surface area and significant sorption capacity, are a good matrix for enzyme immobilization [19]. Among natural carriers for immobilization of naringinase, the following were used: chitin [20], chitosan [21], alginate [22][23][24][25][26][27][28].…”