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- Title
Purification and Properties of an N-acetylglucosaminidase from Streptomyces cerradoensis.
- Authors
da Silva Junior Sobrinho, Iderval; Mendes Bataus, Luiz Artur; Maitan, Valéria Ribeiro; Ulhoa, Cirano José
- 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 m M 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 m M, and was specific to substrates containing acetamide groups such as p-nitrophenyl- β- N-acetylglucosaminide and p-nitrophenyl- β-D- N,N′-diacetylchitobiose.
- Subjects
STREPTOMYCES; BACTERIA; ENZYME activation; ENZYME regulation; ACETAMIDE; BIOTECHNOLOGY
- Publication
Biotechnology Letters, 2005, Vol 27, Issue 17, p1273
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-005-0218-2