Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier.

Joanna Bodakowska-Boczniewicz,Zbigniew Garncarek

doi:10.3390/molecules25122731

Joanna Bodakowska-Boczniewicz, Zbigniew Garncarek

Open Access

https://doi.org/10.3390/molecules25122731

Copy DOI

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.

Highlights

Naringinase is an enzyme complex showing dual activity: α-l-rhamnosidase (EC 3.2.1.40) and β-d-glucosidase (EC 3.2.1.21)
A magnetic carrier obtained on the basis of polyethyleneimine activated locust bean gum was used [40]
The potential use of immobilized enzymes in the food industry requires the use of accessible carriers and cheap immobilization methods

Summary

Introduction

Naringinase is an enzyme complex showing dual activity: α-l-rhamnosidase (EC 3.2.1.40) and β-d-glucosidase (EC 3.2.1.21). Due to the ability to deglycosylate compounds containing α-rhamnose or β-glucose at the end of the molecule, many natural glycosides can be substrates for naringinase [1]. These include, among others: naringin, rutin, quercetin, hespedrin, neohesperidine, diosmin, myricitrin, monoterpenes and some saponins including ginsenosides [2,3,4,5,6,7]. Naringin is a dominant bioflavonoid found in citrus fruit, mainly in grapefruit, giving it a bitter, characteristic taste [8]. Naringinase plays an important role mainly in citrus fruit processing, reducing the intensity of its bitter taste

Objectives

Methods

Results

Conclusion