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J Sci Food Agric. 2013 Dec;93(15):3876-82. doi: 10.1002/jsfa.6363. Epub 2013 Sep 30.

Purification, characterization, and properties of an alkaline protease produced by Serratia marcescens S3-R1 inhabiting Korean ginseng rhizosphere.

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  • 1Department of Animal Bio-system Science, College of Agriculture and Life Sciences, Chungnam National University, Yuseong-gu, Daejeon, 305-764, Republic of Korea.

Abstract

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.

© 2013 Society of Chemical Industry.

KEYWORDS:

Serratia marcescens S3-R1; molecular weight; protease; purification

PMID:
23965944
[PubMed - in process]
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