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Title 

Characterization of a glutamyl aminopeptidase from Bacillus licheniformis NS115

 

Bacillus licheniformis NS115가 생산하는 glutamyl aminopeptidase의 특성

Authors 

Mi Ja ParkJung Kee LeeJong Woo KimHee Sop NamTae Kwang Oh

Publisher 

Korean Journal of Applied Microbiology and Biotechnology

Issue Date 

1998

Citation 

Korean Journal of Applied Microbiology & Biotechnology, vol. 26, no. 5, pp. 420-426

Keywords 

Bacillus licheniformisglutamyl aminopeptidasepurification

Abstract 

An extracellular glutamyl aminopeptidase (EC 3.4.11.7) producing bacterium was isolated from soil and identified as Bacillus licheniformis based on its morphological and physiological characteristics. The aminopeptidase was purified to homogeneity by ammonium sulfate precipitation, Phenyl Sepharose, Resource Q, and Superose 12 column chromatographies. The specific activity of the purified aminopeptidase was 9.2 unit/mg for glutamyl p-nitroanilide with 17.6 purification folds. The purified aminopeptidase had an estimated molecular mass of 64 kDa consists of two different subunits (42 kDa and 22 kDa), and its isoeletric point was 5.2 measured by isoelectric focusing. The optimum pH and temperature of the aminopeptidase were 8.0 and 55°C, respectively. The aminopeptidase was inhibited by EDTA and 1,10- phenanthroline, suggesting it be a metalloenzyme. Comparing with other aminopeptidase, the enzyme showed relatively high activity against peptide having glutamic acid as N-terminal.

ISSN 

0257-2389

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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