Purification and Properties of an <Emphasis Type="Italic">N</Emphasis>-acetylglucosaminidase from <Emphasis Type="Italic">Streptomyces cerradoensis</Emphasis> |
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Authors: | Iderval?da?Silva?Junior?Sobrinho Luiz?Artur?Mendes?Bataus Valéria?Ribeiro?Maitan Email author" target="_blank">Cirano?José?UlhoaEmail author |
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Institution: | (1) Laboratório de Enzimologia, Universidade Federal de Goiás, 74001-970 Goiania, GO, Brazil;(2) Laboratório de Bioquímica e Engenharia Genética, Universidade Federal de Goiás, 74001-970 Goiania, GO, Brazil |
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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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Keywords: | N-acetylglucosaminidase characterization production Streptomyces cerradoensis |
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