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Purification and Properties of an N-acetylglucosaminidase from Streptomyces cerradoensis

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Abstract

An N-acetylglucosaminidase produced by Streptomyces cerradoensis was partially purified giving, by SDS-PAGE analysis, two main protein bands with Mr of 58.9 and 56.4 kDa. The Km and Vmax values for the enzyme using p-nitrophenyl-β-N-acetylglucosaminide as substrate were of 0.13 mM and 1.95 U mg−1 protein, respectively. The enzyme was optimally activity at pH 5.5 and at 50 °C when assayed over 10 min. Enzyme activity was strongly inhibited by Cu2+ and Hg2+ at 10 mM, and was specific to substrates containing acetamide groups such as p-nitrophenyl-β-N-acetylglucosaminide and p-nitrophenyl-β-D-N,N′-diacetylchitobiose.

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Authors and Affiliations

  1. Laboratório de Enzimologia, Universidade Federal de Goiás, 74001-970, Goiânia, GO, Brazil

    Iderval da Silva Junior Sobrinho & Cirano José Ulhoa

  2. Laboratório de Bioquímica e Engenharia Genética, Universidade Federal de Goiás, 74001-970, Goiânia, GO, Brazil

    Luiz Artur Mendes Bataus & Valéria Ribeiro Maitan

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  1. Iderval da Silva Junior Sobrinho
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  2. Luiz Artur Mendes Bataus
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  3. Valéria Ribeiro Maitan
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  4. Cirano José Ulhoa
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Correspondence to Cirano José Ulhoa.

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Sobrinho, I.d.S.J., Bataus, L.A.M., Maitan, V.R. et al. Purification and Properties of an N-acetylglucosaminidase from Streptomyces cerradoensis . Biotechnol Lett 27, 1273–1276 (2005). https://doi.org/10.1007/s10529-005-0218-2

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  • DOI: https://doi.org/10.1007/s10529-005-0218-2

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