Abstract
Previously, we reported that ε-poly-L-lysine (25–35 residues) significantly promoted a glucose oxidase enzymatic (GOx) reaction using ferricyanide ion as the oxidant, and that the effect was due to the formation of a polyion complex between anionic GOx and protonated (polycationic) ε-poly-L-lysine. Here, we show that streptothricins (STs), which have an L-β-lysine oligomer (1–7 residues) and possess only several positive charges at most, also effectively promote the GOx enzymatic reaction. Interestingly, the promotion effect increased with the size of the lysine oligomer of STs, suggesting that the ionic valence is a key factor determining the degree of the promotion effect. The GOx enzymatic reaction is accompanied by a color change due to the reduction of yellow ferricyanide ion to a colorless reductant. A more distinctive color change can be achieved by the addition of Fe(III) ions due to the formation of Prussian blue. Thus, the promotion effect allowed for colorimetric detection of STs at the 1 mg/L level. The detection method was simple and easy to carry out, and would become a helpful tool for the detection of STs.
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References
R. Wilson and A. P. F. Turner, Biosens. Bioelectron., 1992, 7, 165.
A. E. G. Cass, G. Davis, G. D. Francis, H. A. O. Hill, W. J. Aston, I. J. Higgins, E. V. Plotkin, L. D. L. Scott, and A. P. F. Turner, Anal. Chem., 1984, 56, 667.
N. J. Forrow, G. S. Sanghera, and S. J. Walters, J. Chem. Soc., Dalton Trans., 2002, 3187.
E. Liaudet, F. Battaglini, and E. J. Calvo, J. Electroanal. Chem., 1990, 293, 55.
D. M. Fraser, S. M. Zakeeruddin, and M. Graetzel, J. Electroanal. Chem., 1993, 359, 125.
S. Ikeda, T. Yoshioka, and S. Nankai, Denki Kagaku, 1995, 63, 1145.
J. Kulys and N. K. Cenas, Biochim. Biophys. Acta, 1983, 744, 57.
K. Uematsu, M. Yamasaki, T. Hibi, and H. Katano, Anal. Sci., 2012, 28, 657.
K. Uematsu, T. Ueno, K. Ushimaru, C. Maruyama, Y. Hamano, and H. Katano, J. Biosci. Bioeng., 2016, 122, 513.
S. Shima and H. Sakai, Agric. Biol. Chem., 1981, 45, 2503.
H. Katano, T. Yoneoka, N. Kito, C. Maruyama, and Y. Hamano, Anal. Sci., 2012, 28, 1153.
K. Uematsu, Y. Minami, S. Taira, and H. Katano, Anal. Sci., 2014, 30, 299.
Z. Ji, M. Wang, J. Zhang, S. Wei, and W. Wu, J. Antibiot. (Tokyo), 2007, 60, 739.
E.E. van Tamelen, J.R. Dyer, H.A. Whaley, H.E. Carter, and G.B. Whitfield, J. Am. Chem. Soc., 1961, 83, 4295.
Japan Biochemical Society (ed.), “Biochemical Data Book (in Japanese)”, 1979, Vol. 1, Tokyo Kagaku Dojin, Tokyo, 105.
Y. Hamano, N. Matsuura, M. Kitamura, and H. Takagi, J. Biol. Chem., 2006, 281, 16842.
C. Maruyama, J. Toyoda, Y. Kato, M. Izumikawa, M. Takagi, K. Shin-ya, H. Katano, T. Utagawa, and Y. Hamano, Nat. Chem. Biol., 2012, 8, 791.
A. Ahmad, M. S. Akhtar, and V. Bhakuni, Biochemistry, 2001, 40, 1945.
B. E. P. Swoboda and V. Massey, J. Biol. Chem., 1965, 240, 2209.
T. Ikeda, I. Katasho, M. Kamei, and M. Senda, Agric. Biol. Chem., 1984, 48, 1969.
T. Ohgaru, H. Tatsumi, K. Kano, and T. Ikeda, J. Electroanal. Chem., 2001, 496, 37.
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This work was supported in part by JSPS KAKENHI Grants (Nos. 17K14503, 26410226, 16H06445 and 16H03284).
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Uematsu, K., Ueno, T., Kawasaki, H. et al. Promotion Effect of Streptothricin on a Glucose Oxidase Enzymatic Reaction and Its Application to a Colorimetric Assay. ANAL. SCI. 34, 143–148 (2018). https://doi.org/10.2116/analsci.34.143
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DOI: https://doi.org/10.2116/analsci.34.143