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A metallo-keratinase from a newly isolated Acinetobacter sp. R-1 with low collagenase activity and its biotechnological application potential in leather industry


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 Ca2+, 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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This work was financially supported by the National High Technology Research and Development Program of the People’s Republic China (No. 2012AA022204C), and the Ministry of Education of the People’s Republic of China (No. JUSRP51516).

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Correspondence to Jin-Song Shi or Zheng-Hong Xu.

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Zhang, R., Gong, J., Zhang, D. et al. A metallo-keratinase from a newly isolated Acinetobacter sp. R-1 with low collagenase activity and its biotechnological application potential in leather industry. Bioprocess Biosyst Eng 39, 193–204 (2016).

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  • Acinetobacter sp. R-1
  • Keratinase
  • Purification
  • Dehairing
  • Surface modification