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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. Copyright © 2012 Elsevier Ltd. All rights reserved.

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Jizheng Dang, Hongbo Liu, Xiaolan Yang, Yi Zhang, Yanling Xie, Yuanli Li, Jun Pu, Juan Liao, Yonghua Yuan, Fei Liao. 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. Bioorganic & medicinal chemistry letters. 2013 Feb 1;23(3):646-9

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PMID: 23267768

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