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J Sci Food Agric ; 93(15): 3876-82, 2013 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-23965944

RESUMEN

BACKGROUND: An alkaline protease produced by the Serratia marcescens S3-R1 which inhabits in the Korean ginseng rhizosphere was investigated. The purposes of this study were to characterize and purify the bacterial enzyme by four different purification steps: precipitation of enzyme fraction by ammonium sulfate, loading the enzyme pellets on a DEAE-Sepharose anion-exchange chromatograph, separation of the fraction containing enzyme activity by fast protein liquid Mono Q chromatography and identification of the single-band fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and then quantification of the single-band fraction by reverse-phase high-performance liquid chromatography. RESULTS: The molecular weight of the purified protease was estimated as 50 308 Da by matrix-assisted laser desorption ionization time-of-flight analysis. The N-terminal amino acid sequence of the protease was identified as Ala-Val-Thr-Ile-Glu-Asp-Ala-Val-Asp-Asp, and the enzyme belongs to the metalloprotease family. The optimal activities of the protease occurred at pH 7-9 and a temperature 40 °C. The ranges of pH and thermal stability of the enzyme were at 7-10 and 30-40 °C, respectively. CONCLUSION: The alkaline protease was successfully purified and characterized from the bacterium Serratia marcescens S3-R1, which has potential for industrial application, including milk protein hydrolysates.


Asunto(s)
Proteínas Bacterianas/aislamiento & purificación , Endopeptidasas/aislamiento & purificación , Panax/microbiología , Raíces de Plantas/microbiología , Rizosfera , Serratia marcescens/enzimología , Microbiología del Suelo , Secuencia de Aminoácidos , Proteínas Bacterianas/química , Endopeptidasas/química , Concentración de Iones de Hidrógeno , Peso Molecular , Temperatura
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