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Over-Expression of the Thermobifida fusca β-Glucosidase in a Yarrowia lipolytica Transformant to Degrade Soybean Isoflavones

Department of Applied Chemistry, Providence University, Taichung 43301, Taiwan
Department of Cosmetic Science, Providence University, Taichung 43301, Taiwan
Department of Biochemical Science and Technology, National Taiwan University, Taipei 10617, Taiwan
Xtremes Pure Company, Taipei 10652, Taiwan
Author to whom correspondence should be addressed.
Catalysts 2018, 8(1), 24;
Received: 4 January 2018 / Revised: 12 January 2018 / Accepted: 12 January 2018 / Published: 14 January 2018
(This article belongs to the Special Issue Novel Enzyme and Whole-Cell Biocatalysis)
PDF [1679 KB, uploaded 14 January 2018]


A gene (bgl) encoding a β-glucosidase in thermophilic actinomycete Thermobifida fusca NTU 22 was cloned into a Yarrowia lipolytica expression system. Heterologous expression resulted in extracellular β-glucosidase production with activity as high as 630 U/mL in a Hinton flask culture filtrate. This recombinant β-glucosidase was purified 9.2-fold from crude culture filtrate by DEAE-Sepharose FF column chromatography as measured by its increase in specific activity. The overall yield of the purified enzyme was 47.5%. The molecular weight of the purified β-glucosidase estimated by SDS-PAGE was 45 kDa, which agreed with the predicted molecular weight based on the nucleotide sequence. About 15% enzyme activity loss was observed after the enzyme was heat-treated at 50 °C for 180 min. It was also found that the activity of the enzyme was inhibited by Hg2+, Cu2+, Ba2+, Ag+, p-chloromercuribenzene, and iodoacetate. The β-glucosidase from T. fusca had the most activity for daidzein-7-glucoside and genistein-7-glucoside among the tested flavonoid glycosides, but there was moderate or little activity for luteolin-7-glucoside, cyanidine-3-glucoside, and quercetin-3-glucoside. These properties are important for the soybean isoflavone applications of this β-glucosidase. View Full-Text
Keywords: Thermobifida fuscal; β-glucosidase; Yarrowia lipolytica; daidzin; genistin Thermobifida fuscal; β-glucosidase; Yarrowia lipolytica; daidzin; genistin

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Chen, W.-L.; Yang, Y.-M.; Guo, G.-W.; Chen, C.-Y.; Huang, Y.-C.; Liu, W.-H.; Huang, K.-F.; Yang, C.-H. Over-Expression of the Thermobifida fusca β-Glucosidase in a Yarrowia lipolytica Transformant to Degrade Soybean Isoflavones. Catalysts 2018, 8, 24.

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