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.
Highlights
Microorganisms are used in various fields especially in industries due to their ability to produce various enzymes, among these enzymes is naringinase one of the great important enzymes (Deene and Lingappa 2013).Naringinase (EC3.2.1.40) is a hydrolytic enzyme containing both a-L-rhamnosidase and b-glucosidase activities
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
A-L-rhamnosidase hydrolyzes naringin into rhamnose and prunin (4,5,7-trihydroxy flavanone-7-glucoside), the prunin is simultaneously converted into glucose and naringenin (4,5,7-trihydroxy flavanone) by the b-glucosidase activity (Yusof et al 1990)
Summary
Microorganisms are used in various fields especially in industries due to their ability to produce various enzymes, among these enzymes is naringinase one of the great important enzymes (Deene and Lingappa 2013).Naringinase (EC3.2.1.40) is a hydrolytic enzyme containing both a-L-rhamnosidase and b-glucosidase activities. A-L-rhamnosidase hydrolyzes naringin into rhamnose and prunin (4,5,7-trihydroxy flavanone-7-glucoside), the prunin is simultaneously converted into glucose and naringenin (4,5,7-trihydroxy flavanone) by the b-glucosidase activity (Yusof et al 1990). Naringin is the source of undesirable bitterness especially in citrus fruit juice industry; it must be removed or reduced its levels from the processed products (Yusof et al 1990; Hasegawa and Maier 1993).
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