Biotechnology Letters

, Volume 27, Issue 17, pp 1273–1276 | Cite as

Purification and Properties of an N-acetylglucosaminidase from Streptomyces cerradoensis

  • Iderval da Silva Junior Sobrinho
  • Luiz Artur Mendes Bataus
  • Valéria Ribeiro Maitan
  • Cirano José Ulhoa
Article

Abstract

An N-acetylglucosaminidase produced by Streptomycescerradoensis 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.

Keywords

N-acetylglucosaminidase characterization production Streptomyces cerradoensis 

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Copyright information

© Springer 2005

Authors and Affiliations

  • Iderval da Silva Junior Sobrinho
    • 1
  • Luiz Artur Mendes Bataus
    • 2
  • Valéria Ribeiro Maitan
    • 2
  • Cirano José Ulhoa
    • 1
  1. 1.Laboratório de EnzimologiaUniversidade Federal de GoiásGoiâniaBrazil
  2. 2.Laboratório de Bioquímica e Engenharia GenéticaUniversidade Federal de GoiásGoiâniaBrazil

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