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Title 

Purification and properties of an extracellular leucine aminopeptidase from the Bacillus sp. N2

Authors 

G D LeeS S ChunYung Hee KhoHyo Kon Chun

Publisher 

Wiley-Blackwell

Issue Date 

1998

Citation 

Journal of Applied Microbiology, vol. 84, no. 0, pp. 561-566

Keywords 

cytosol aminopeptidasebacillusenzyme specificityprotein purification

Abstract 

A halophilic bacterium was isolated from fermented anchovy sauce and identified as Bacillus species. An extracellular leucine aminopeptidase from Bacillus sp. N2 was purified to homogeneity using four successive purification steps. The enzyme has a native molecular mass of about 57 000 Da using FPLC gel filtration analysis and a molecular mass of 58 000 Da using SDS-polyacrylamide gel electrophoresis. This monomeric leucine aminopeptidase showed maximum enzyme activity at pH 9.5. The optimum temperature was 50 °C when L-Leu-p-nitroanilide was the substrate. The leucine aminopeptidase was inactivated by 1,10-phenanthroline, dithiothreitol and sodium dodecyl sulphate. Enzyme activity was increased by addition of Co2+. It is likely that Co2+ plays an important role in the catalysis or stability of the Bacillus sp. N2 leucine aminopeptidase. Sodium chloride (0-4.5 mol l-1) increased the hydrolytic activity towards L-Leu-p-nitroanilide. The N- terminal amino acid sequence was Glu-Arg-Glu-Leu-Pro-Phe-Lys-Ala-Lys-His- Ala-Tyr-Ser-Thr-Ile. The purified enzyme had a high specificity for L-Leu-p- nitroanilide.

ISSN 

1364-5072

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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