Optimization of Process Parameters by Statistical Experimental Designs for the Production of Naringinase Enzyme by Marine Fungi

Abeer Nasr Shehata,Abeer Abas Abd El Aty

doi:10.1155/2014/273523

Abeer Nasr Shehata, Abeer Abas Abd El Aty

Open Access

https://doi.org/10.1155/2014/273523

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Abstract

Naringinase has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose and prunin and debittering of citrus fruit juices. Screening of fifteen marine-derived fungi, locally isolated from Ismalia, Egypt, for naringinase enzyme production, indicated thatAspergillus nigerwas the most promising. In solid state fermentation (SSF) of the agroindustrial waste, orange rind was used as a substrate containing naringin. Sequential optimization strategy, based on statistical experimental designs, was employed to enhance the production of the debittering naringinase enzyme. Effects of 19 variables were examined for their significance on naringinase production using Plackett-Burman factorial design. Significant parameters were further investigated using Taguchi’s (L1645) orthogonal array design. Based on statistical analysis (ANOVA), the optimal combinations of the major constituents of media for maximal naringinase production were evaluated as follows: 15 g orange rind waste, 30 mL moisture content, 1% grape fruit, 1% NaNO3, 0.5% KH2PO4, 5 mM MgSO4, 5 mM FeSO4, and the initial pH 7.5. The activity obtained was more than 3.14-fold the basal production medium.

Highlights

Naringinase, an α-rhamnopyranosidase, expressed as αL-rhamnosidase (E.C. 3.2.1.40) and β-D-glucosidase (E.C. 3.2.1.21) activities
Fifteen marine-derived fungi were screened for naringinase enzyme production
Four identified as Aspergillus niger, Penicillium nalgiovense, Aspergillus flavus, and Aspergillus terreus are capable of producing naringinase enzyme on orange rind substrate (4.42, 4.16, 0.03, and 0.03 U/mL, resp.)

Summary

Introduction

Naringinase, an α-rhamnopyranosidase, expressed as αL-rhamnosidase (E.C. 3.2.1.40) and β-D-glucosidase (E.C. 3.2.1.21) activities This hydrolytic enzymatic complex has wide occurrence in nature and has been reported in plants, yeasts, fungi, and bacteria [1]. The former enzyme splits naringin into rhamnose and prunin and the latter further hydrolyses prunin to D-glucose and naringenin, a nonbitter component, which cannot be converted back to naringin [2, 3]. Naringinase is commercially attractive due to its potential usefulness in pharmaceutical and food industries It is of particular interest in the biotransformation of steroids and antibiotics and mainly on glycosides hydrolysis. It has been used in citrus juices debittering and wine industries [4, 5]

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