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The production of flavonoid glycosides by removing rhamnose from rutinosides can be accomplished through enzymatic catalysis. Naringinase is an enzyme complex, expressing both  α -L-rhamnosidase and  β -D-glucosidase activities, with application in glycosides hydrolysis. To produce monoglycosylated flavonoids with naringinase, the expression of  β -D-glucosidase activity is not desirable leading to the need of expensive methods for  α -L-rhamnosidase purification. Therefore, the main purpose of this study was the inactivation of  β -D-glucosidase activity expressed by naringinase keeping  α -L-rhamnosidase with a high retention activity. Response surface methodology (RSM) was used to evaluate the effects of temperature and pH on  β -D-glucosidase inactivation. A selective inactivation of  β -D-glucosidase activity of naringinase was achieved at 81.5°C and pH 3.9, keeping a very high residual activity of  α -L-rhamnosidase (78%). This was a crucial achievement towards an easy and cheap production method of very expensive flavonoids, like prunin and isoquercetin starting from naringin and rutin, respectively.

enzyme research

Enzymatic Synthesis of the Flavone Glucosides, Prunin and Isoquercetin, and the Aglycones, Naringenin and Quercetin, with Selective <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi mathvariant="bold">α</mml:mi></mml:math>-L-Rhamnosidase and <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi mathvariant="bold">β</mml:mi></mml:math>-D-Glucosidase Activities of Naringinase

Enzymatic Synthesis of the Flavone Glucosides, Prunin and Isoquercetin, and the Aglycones, Naringenin and Quercetin, with Selective α-L-Rhamnosidase and β-D-Glucosidase Activities of Naringinase