Naringinase-catalyzed hydrolysis of naringin adsorbed on macroporous resin |
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| Affiliation: | 1. College of Food and Biological Engineering, Jimei University, Xiamen 361021, China;2. Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen, Fujian Province 361021, China;3. Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen, Fujian Province 361021, China;4. Xiamen Key Laboratory of Marine Functional Food, Xiamen 361021, China;1. INCITAP—CONICET (National Scientific and Technical Research Council), Department of Chemistry, Faculty of Natural Sciences, National University of La Pampa (UNLPam), Av. Uruguay 151, 6300 Santa Rosa, La Pampa, Argentina;2. Sustainable Momentum, SL. Ap. Correos 3517, 35004 Las Palmas de Gran Canaria, Canary Islands, Spain;1. City University of Hong Kong, Hong Kong;2. University of Wisconsin, Madison and NBER, United States;3. Barclays, United Kingdom;4. Center for Healthcare Policy and Research, University of California, Davis, One Shields Avenue, Davis, CA 95616, United States;1. Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, 159 Long Pan Road, Nanjing, 210037, China;2. College of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China |
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| Abstract: | Naringenin, a natural plant flavonoid found in citrus fruits, has been reported to exhibit a wide range of pharmacological functions, including anticancer, antioxidant, antiatherogenic, antithrombotic, and vasodilator activities. Naringenin can be produced from the naringinase (NGase)-catalyzed enzymatic hydrolysis of naringin. However, the poor solubility of naringin in aqueous systems considerably limits the efficiency of naringenin biocatalysis. In this work, a novel substrate adsorption system was proposed for naringin adsorption to increase the efficiency of naringin hydrolysis and naringenin production. Three Amberlite macroporous resins, namely, XAD-4, XAD-7HP and XAD-16, were investigated for their naringin adsorption capacities and effects on NGase hydrolysis. Results indicated that the physical properties of the resins played a critical role in naringin adsorption and naringenin enzymatic synthesis. Naringin hydrolysis was carried out using free and adsorbed substrates. The substrate adsorption strategy could increase the catalytic efficiency at a high naringin concentration. In addition, the reaction conditions for enzymatic naringenin synthesis were optimized, and naringenin was prepared at a liter scale with a high substrate concentration. These results suggested that substrate adsorption is a promising strategy to increase the enzymatic hydrolysis efficiency of naringenin in aqueous systems. |
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| Keywords: | Naringin Naringenin Naringinase Substrate adsorption |
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