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. 2005 Sep;27(17):1273-6.
doi: 10.1007/s10529-005-0218-2.

Purification and properties of an N-acetylglucosaminidase from Streptomyces cerradoensis

Iderval da Silva Sobrinho Jr  1 , Luiz Artur Mendes Bataus, Valéria Ribeiro Maitan, Cirano José Ulhoa
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Purification and properties of an N-acetylglucosaminidase from Streptomyces cerradoensis

Iderval da Silva Sobrinho Jr et al. Biotechnol Lett. 2005 Sep.

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-beta-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 degrees 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-beta-N-acetylglucosaminide and p-nitrophenyl-beta-D-N,N'-diacetylchitobiose.

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