Chromogenic substrate from 4-nitro-1-naphthol for hydrolytic enzyme of neutral or slightly acidic optimum pH: 4-Nitro-1-naphthyl-β-d-galactopyranoside as an example

doi:10.1016/j.bmcl.2012.11.120

Bioorganic & Medicinal Chemistry Letters

Volume 23, Issue 3, 1 February 2013, Pages 646-649

https://doi.org/10.1016/j.bmcl.2012.11.120 Get rights and content

Abstract

At pH from 5.5 to 7.6, absorptivity of 4-nitro-1-naphthol at 450 nm is over 2.1-fold of that of para-nitrophenol at 405 nm and over 9.6-fold of that of ortho-nitrophenol at 415 nm. On 4-nitro-1-naphthyl-β-d-galactopyranoside at pH 7.4, catalytic efficiency of Escherichia coli β-d-galactosidase is 3-fold of that on para-nitrophenyl-β-d-galactopyranoside and about 40% of that on ortho-nitrophenyl-β-d-galactopyranoside, and produces a lower quantification limit of penicillin G by enzyme-linked-immunoabsorbent-assay. Hence, 4-nitro-1-naphthol is favorable to prepare chromogenic substrates of hydrolytic enzymes of neutral or slightly acidic optimum pH.

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Acknowledgments

This project was supported by ‘863’-High-Technology Program (No. 2011AA02A108), the program for New Century Excellent Talent in University (NCET-09-0928), National Natural Science Foundation of China (No. 81071427) and Natural Science Foundation Project of CQ (CSTC2011BA5039, CSTC2012JJA081).

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^†: These authors contributed equally to this work.

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Chromogenic substrate from 4-nitro-1-naphthol for hydrolytic enzyme of neutral or slightly acidic optimum pH: 4-Nitro-1-naphthyl-β-d-galactopyranoside as an example

Abstract

Graphical abstract

Section snippets

Acknowledgments

Methods Enzymol.

Curr. Opin. Chem. Biol.

J. Virol. Methods

Bioorg. Med. Chem. Lett.

Biochim. Biophys. Acta

Carbohydr. Res.

J. Ind. Microbiol. Biotechnol.