Biotransformation of rutin to isoquercitrin using recombinant α-L-rhamnosidase from Bifidobacterium breve

Biotechnology Letters
Ru ZhangYu-Ting Xiang

Abstract

To biotransform rutin into isoquercitrin. A α-L-rhamnosidase from Bifidobacterium breve was produced by using Escherichia coli BL21 for biotransformation of rutin to isoquercitrin. The enzyme was purified by Ni(2+)-NTA chromatography to yield a soluble protein with a specific activity of 56 U protein mg(-1). The maximum enzyme activities were at pH 6.5, 55 °C, 20 mM rutin, and 1.2 U enzyme ml(-1). Under optimal conditions, the half-life of the enzyme was 96 h. The K m and V max values were 2.2 mM, 56.4 μmol mg(-1) min(-1) and 2.1 mM, 57.5 μmol mg(-1) min(-1) using pNP-Rha and rutin as substrates, respectively. The kinetic behavior indicated that the recombinant α-L-rhamnosidase has good catalytic performance for producing isoquercitrin. 20 mM rutin was biotransformed into 18.25 and 19.87 mM isoquercitrin after 60 and 240 min. The specific biotransformation of rutin to isoquercitrin using recombinant α-L-rhamnosidase from B. breve is a feasible method for use in industrial processes.

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Citations

Aug 31, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Rosario RussoNunziatina De Tommasi
Nov 6, 2018·Acta Crystallographica. Section D, Structural Biology·Petr PachlPavlína Řezáčová
Nov 11, 2017·Bioprocess and Biosystems Engineering·Monika MuellerFrank M Unger
Nov 6, 2015·Frontiers in Microbiology·Kristína MarkošováMartin Rebroš
Jun 5, 2019·Applied Biochemistry and Biotechnology·Deqing WangPengcheng Chen
Aug 7, 2019·Applied Biochemistry and Biotechnology·Ping SunKequan Chen

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