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

作者：Zhang, Rong-Xian; Gong, Jin-Song; Zhang, Dan-Dan; Su, Chang; Hou, Ying-Shuo; Li, Heng; Shi, Jin-Song^*; Xu, Zheng-Hong

来源：Bioprocess and Biosystems Engineering, 2016, 39(1): 193-204.

DOI：10.1007/s00449-015-1503-7

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

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 A degrees 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.

• 出版日期2016-1
• 单位江南大学