Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin.
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.
Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, Egypt.
Ghada E A
GEA
Awad
Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, Egypt. aabass44@yahoo.com.
Abeer A
AA
Abd El Aty
Biochemistry Department, National Research Centre, Dokki, Giza, Egypt. futtur@yahoo.com.
Abeer N
AN
Shehata
Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, Egypt.|Encapsulation and Nanobiotechnology Group, Center of Excellence, National Research Centre, Dokki, Giza, Egypt.
Mohamed E
ME
Hassan
Biomedical Sciences Department, Curtin University, Perth, Australia.|Polymers Department, National Research Centre, Dokki, Giza, Egypt.|Encapsulation and Nanobiotechnology Group, Center of Excellence, National Research Centre, Dokki, Giza, Egypt.
Magdy M
MM
Elnashar
ART-FTIR (total reflectance Fourier transform infrared); Aspergillus niger; Immobilization; Naringinase; TGA (thermal gravimetric analysis) and biopolymer (grafted alginate gel beads)