Purification and properties of an N-acetylglucosaminidase from Streptomyces cerradoensis.
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.
da Silva Sobrinho
Iderval
I
Laboratório de Enzimologia, Universidade Federal de Goiás, 74001-970, Goiânia, GO, Brazil.
Bataus
Luiz Artur Mendes
LA
Maitan
Valéria Ribeiro
VR
Ulhoa
Cirano José
CJ
D000118:Acetylglucosaminidase / Q000737:chemistry* / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D000118:Acetylglucosaminidase