Characterization of a novel <Emphasis Type="Italic">Stenotrophomonas</Emphasis> isolate with high keratinase activity and purification of the enzyme |
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Authors: | Zhang-Jun Cao Qi Zhang Dong-Kai Wei Li Chen Jing Wang Xing-Qun Zhang Mei-Hua Zhou |
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Institution: | (1) Key Laboratory of Science and Technology of Eco-Textile, Donghua University, Ministry of Education, 201620 Shanghai, China;(2) College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 201620 Shanghai, China;(3) College of Environmental Science and Engineering, Donghua University, 201620 Shanghai, China |
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Abstract: | A feather-degrading bacterium was isolated from poultry decomposition feathers in China. The strain, named L1, showed significant
feather-degrading activity because it grew and reproduced quickly on basal medium containing 10 g/L of native feather as the
source of energy, carbon, and nitrogen. According to the phenotypic characteristics and 16S rRNA profile, the isolate belongs
to Stenotrophomonas maltophilia. Keratinase activity of the isolate was determined during cultivation on raw feathers at different temperatures and initial
pH. Maximum growth and feather-degrading activity of the bacterium were observed at 40°C and initial pH ranging from 7.5 to
8.0. The crude enzyme was purified by ammonium sulphate precipitation, Sephadex G-100 chromatographic and ceramic hydroxyapatite
(CHT) chromatographic. Its molecular mass estimated as 35.2 kDa in SDS-PAGE. The enzyme had an optimum activity at the pH
was 7.8 and the temperature was 40°C. The keratinase was wholly inhibited by a serine protease inhibitor, PMSF. Its activity
was activated or inhibited by different metal ions. The keratinase activity of enzyme from strain L1 functioned on different
keratins, such as feather, hair, wool, horn, and so on. |
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Keywords: | Keratin-degrading bacterium Feather 16S rRNA Cultivated conditions Keratinase characteristics |
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