Selective synthesis of citrus flavonoids prunin and naringenin using heterogeneized biocatalyst on graphene oxide

Abstract

Citrus flavonoids, prunin and naringenin, are selectively produced from hydrolysis of naringin using the enzyme naringinase supported on graphene oxide.

A Novel and High-Effective Biosynthesis Pathway of Hesperetin-7-O-Glucoside Based on the Construction of Immobilized Rhamnosidase Reaction Platform

“…Chen and Zhu (2018) The product purity of zinc-hesperidin complex prepared by solution coordination was lower than that prepared by separation and integration method. Carceller et al (2019) In this paper, GO was used to immobilize rhamnosidase for selective synthesis of citrus flavonoids prunin and naringenin, but no magnetic separation.…”

“…Flavanones belong to a unique class of polyphenols containing three main aglycones: hesperetin, eriodictyol and naringenin (Manach et al, 2003). These glycosylated flavonoids are important components of citrus and play a vital role in human health (Carceller et al, 2019). Hesperidin, has been identified as the most abundant flavonoid in citrus peel, followed by naringin, a derivative of hesperidin (Nogata et al, 2006).…”

“…The hydrolysis of rhamnoside has crucial application values in debittering grapefruit juice and other citrus juices (Birgisson et al, 2007;Soria et al, 2012). Besides, there are other applications in the following: enhancing the wine aroma after hydrolysis of terpene glycoside precursors (Manzanares et al, 2003), using as an agent for structural study of glycosides to hydrolyzes L-rhamnosides specifically (Monti et al, 2004), and preparation of raw materials to synthesize several compounds of prospect in the food industry by hydrolysis of natural glycosides (Carceller et al, 2019).…”

Covalent Immobilization of Naringinase over Two‐Dimensional 2D Zeolites and its Applications in a Continuous Process to Produce Citrus Flavonoids and for Debittering of Juices

“…The purification of naringinase was performed following the literature. [19] A solution of naringinase (500 mg in 50 mL of milliQ water) was added to the resin (chromatographic resin DEAE-Sephacel) previously equilibrated with 5 mM NaH 2 PO 4 buffer pH 6.8) and maintained under gentle stirring for 1 hour. The adsorption of the enzyme was monitored by protein quantification using bicinchoninic acid protein test.…”

“…Additionally, immobilization can decrease inhibition problems, resistance to chemicals or increase enzyme purity. [7,8] Particularly, naringinase has been supported on a variety of materials such as tannin-aminohexylcellulose, [9] chitin, [10] cellulose acetate films, [11] glutaraldehyde coated wood chips, [12] structured mesoporous silicates such as MCM-41, [13] and SBA-15, [14] over sol-gel of polyvinyl alcohol (PVA), [15,16] electrospun cellulose acetate nanofibers, [17] graphene, [18] and graphene oxide [19] while the enzyme has also been entrapped with sodium or potassium alginate. [20][21][22] Compared with conventional supports, nanostructured materials possess interesting properties such as their high specific surface area that is beneficial for improving the immobilization efficiency.…”