China
Africa
Explore chapters and articles related to this topic
Transformation of Natural Products by Marine-Derived Microorganisms
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Thayane Melo de Queiroz, André Luiz Meleiro Porto
De Lise and co-workers (2016) described the isolation, recombinant expression in E. coli, and partial characterisation of a α-L-rhamnosidase (α-RHA) obtained from the marine bacteria Novosphingobium sp. PP1Y, which was isolated from surface seawater (Italy). In this study, the α-RHA enzyme was used in the hydrolysis of the flavonoids naringin, rutin, and neohesperidin dihydrochalcone into their glycosylated derivatives. The reactions were performed in Na-phosphate buffer (pH 7.0) under magnetic stirring at 40°C for 1–3 hours (Figure 5.9).
Preparation of isoquercitrin by biotransformation of rutin using α-L-rhamnosidase from Aspergillus niger JMU-TS528 and HSCCC purification
Published in Preparative Biochemistry & Biotechnology, 2020
Li Jun Li, Xiao Qing Liu, Xi Ping Du, Ling Wu, Ze Dong Jiang, Hui Ni, Qing Biao Li, Feng Chen
In industry, isoquercitrin is prepared by hydrolyzing the terminal rhamnose from rutin by means of acid hydrolysis,[16] heating,[14] microbial transformation,[17,18] or enzymatic transformation.[16,19] Among these, acidic and thermal hydrolyzes nonspecifically hydrolyze the rhamnoside bond and the glucoside bond, which simultaneously yields quercetin and isoquercitrin, decreasing the isoquercitrin productivity and increasing the purification cost.[16] Enzymes such as naringinase, hesperidinase, and α-L-rhamnosidase (Fig. 1) have been proposed for transforming rutin to isoquercitrin.[9,14,20–23] Naringinase and hesperidinase also yield quercetin and isoquercitrin simultaneously,[24,25] as they have the activities of both α-L-rhamnosidase and β-D-glucosidase.[19] In contrast, the enzyme α-L-rhamnosidase specifically hydrolyzes the terminal L-rhamnose from natural glycosides, which avoid the generation of quercitrin and thus transform rutin solely to isoquercitrin. Some α-L-rhamnosidases were reported to transform rutin to isoquercitrin;[26] however, the low enzyme activity or low affinity of the enzyme to rutin resulted in a low transformation rate, causing difficulties in purification. Therefore, various purification methods are involved in the preparation of isoquercitrin, leading to long purification times and high production costs.[21] For instance, Li et al. applied macroporous adsorptive resin column chromatography in combination with Sephadex LH-20 column chromatography to purify isoquercitrin.[27] Wen et al. developed a combined procedure consisting of high-speed countercurrent chromatography (HSCCC) and preparative high-performance liquid chromatography to purify isoquercitrin.[28]