Covalent Immobilization of Microbial Naringinase Using Novel Thermally Stable Biopolymer for Hydrolysis of Naringin

Overview

Journal 3 Biotech

Publisher Springer

Specialty Biotechnology

Date 2017 Mar 24

PMID 28330084

Citations 12

Authors

Ghada E A Awad

Abeer A Abd El Aty

Abeer N Shehata

Mohamed E Hassan

Magdy M Elnashar

Affiliations

Soon will be listed here.

Abstract

Naringinase induced from the fermented broth of marine-derived fungus Aspergillus niger was immobilized into grafted gel beads, to obtain biocatalytically active beads. The support for enzyme immobilization was characterized by ART-FTIR and TGA techniques. TGA revealed a significant improvement in the grafted gel's thermal stability from 200 to 300 °C. Optimization of the enzyme loading capacity increased gradually by 28-fold from 32 U/g gel to 899 U/g gel beads, retaining 99 % of the enzyme immobilization efficiency and 88 % of the immobilization yield. The immobilization process highly improved the enzyme's thermal stability from 50 to 70 °C, which is favored in food industries, and reusability test retained 100 % of the immobilized enzyme activity after 20 cycles. These results are very useful on the marketing and industrial levels.

Citing Articles

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