Abstract
Objectives
To optimize conversion of rutin to isoquercetin by commercial α-l-rhamnosidase using high hydrostatic pressure (HHP).
Results
The de-rhamnosylation activity of α-l-rhamnosidase for isoquercetin production was maximal at pH 6.0 and 50 °C using HHP (150 MPa). The enzyme showed high specificity for rutin. The specific activity for rutin at HHP was 1.5-fold higher than that at atmospheric pressure. The enzyme completely hydrolysed 20 mM rutin in tartary buckwheat extract after 2 h at HHP, with a productivity of 10 mM h−1. The productivity and conversion were 2.2- and 1.5-fold higher at HHP than at atmospheric pressure, respectively.
Conclusions
This is the first report concerning the enzymatic hydrolysis of isoquercetin in tartary buckwheat at HHP.
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Acknowledgments
This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (grant number 2015R1D1A1A01059570).
Supplementary Information
Supplementary Fig. 1—Effect of enzyme concentration on isoquercetin production by commercial α-l-rhamnosidase. The reactions were performed in 50 mM McIlvaine buffer (pH 6.0) containing 0.5–4 U enzyme ml −1 and 20 mM rutin with 5 % DMSO at 50 °C for 3 h. Error bars indicate the standard deviations of triplicate samples.
Supplementary Fig. 2—Effect of substrate (rutin) concentration on isoquercetin production by commercial α-l-rhamnosidase. The reactions were performed in 50 mM McIlvaine buffer (pH 6.0) containing 3 U enzyme ml −1 and 1–20 mM rutin with 5 % DMSO at 50 °C for 3 h. Error bars indicate the standard deviations of triplicate samples.
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Kim, DY., Yeom, SJ., Park, CS. et al. Effect of high hydrostatic pressure treatment on isoquercetin production from rutin by commercial α-l-rhamnosidase. Biotechnol Lett 38, 1775–1780 (2016). https://doi.org/10.1007/s10529-016-2157-5
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DOI: https://doi.org/10.1007/s10529-016-2157-5