Minor thermodtable alkaline protease produced by Thermoactinomyces sp. E79

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Title
Minor thermodtable alkaline protease produced by Thermoactinomyces sp. E79
Author(s)
Young Ok Kim; Jung Kee Lee; Kandula Sunitha; Hyung Kwoun Kim; Tae Kwang Oh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 9, no. 4, pp. 469-474
Publication Year
1999
Abstract
Thermoactinomyces sp. E79 produced two types of thermostable alkaline proteases extracellularly. A minor protease was separated from a major protease by using DEAE-column chromatography. This enzyme was purified to homogeneity by ammonium sulfate and DEAE-Sepharose ion-exchange chromatography. The purified minor protease showed different biochemical properties compared to the major protease. The molecular mass of the purified enzyme was estimated by SDS-PAGE to be 36 kDa. Its optimum temperature and pH for proteolytic activity against Hammarsten casein were 70°C and 9.0, respectively. The enzyme was stable up to 75°C and in an alkaline pH range of 9.0-11.0. The enzyme was inhibited by phenylmethylsulfonyl fluoride (PMSF) and Hg2+, indicating that the enzyme may be a cysteine-dependent serine protease. In addition, the enzyme cleaved the endoproteinase substrate, succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and the K(m) value for the substrate was 1.2 mM.
Keyword
thermoactinomycesthermophilealkaline proteasethermostable enzymepurification
ISSN
1017-7825
Publisher
South Korea
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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