4.4 Article

Purification and characterization of an extracellular chitinase from antagonistic Streptomyces violaceusniger

期刊

JOURNAL OF BASIC MICROBIOLOGY
卷 53, 期 5, 页码 429-439

出版社

WILEY
DOI: 10.1002/jobm.201100648

关键词

Streptomyces violaceusniger; Purification; Chitinase; Biocontrol; MALDI-TOF

资金

  1. Ministry of Environment and Forests, India [19-35/2008-RE]

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The actinomycetes Streptomyces violaceusniger showed strong antagonistic activity against various tested wood rotting fungi. An extracellular chitinase, produced by antagonistic S. violaceusniger MTCC 3959, was purified as follows: ammonium sulfate precipitation, chitin affinity and chromatographic separation of Q Sepharose. The molecular mass of the purified chitinase was estimated as 56.5kDa by SDS-PAGE. Chitinase was optimally active at pH of 5.0 and 50 degrees C. It retained almost 100% activity at pH 5.0 and also had high thermal tolerance at 50 degrees C. Enzyme activity was inhibited by Hg2+ and Ag+ cations, but was neither substantially inhibited by K+ cation nor by chelating agent EDTA. The apparent Km and Vmax at 37 degrees C were 0.1426mM and 6.6U/mg, respectively using pNP-(GlcNAc)2 as substrate. The 56.5kDa chitinase of strain MTCC 3959 represented an exo-type activity. The purified chitinase was further identified by MALDI-TOF. The results of peptide mass fingerprinting showed that 10 tryptic peptides of the chitinase were identical to the chitinase C from Streptomyces albus J1074 (GenBank Accession No. gi|239982330). The sequence of N-terminal amino acid (AA) of the chitinase was determined to be G-D-G-T-G-P-G-P-G-P.

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