Title |
A metallo-keratinase from a newly isolated Acinetobacter sp. R-1 with low collagenase activity and its biotechnological application potential in leather industry
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Published in |
Bioprocess and Biosystems Engineering, November 2015
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DOI | 10.1007/s00449-015-1503-7 |
Pubmed ID | |
Authors |
Rong-Xian Zhang, Jin-Song Gong, Dan-Dan Zhang, Chang Su, Ying-Shuo Hou, Heng Li, Jin-Song Shi, Zheng-Hong Xu |
Abstract |
Microbial keratinase is a well-recognized enzyme that can specifically degrade insoluble keratins. A keratinase-producing bacterium was isolated from a duck ranch soil and identified as Acinetobacter sp. R-1 based on the biochemical characteristics and 16S rDNA gene sequencing. It showed high keratinase activity and low collagenase activity. The keratinase was purified to electrophoretic homogeneity with 6.69 % recovery, 2.68-fold purification and an estimated molecular weight of 25 kDa. Additionally, the keratinase showed optimal activity at 50 °C and pH11. Keratinase activity of Acinetobacter sp. significantly increased in the presence of Li(+), Na(+), and Ca(2+), while it was completely inhibited by EDTA, indicating it was a metallo-keratinase. Moreover, the crude keratinase from Acinetobacter sp. R-1 could thoroughly depilate goat skin and simultaneously modify the wool surface, which indicated its applicable potential in leather and textile industries. |
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Unknown | 9 | 38% |