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Received June 30, 2015
Accepted August 28, 2015
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This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits
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A facile technique to prepare cross-linked enzyme aggregates of bovine pancreatic lipase using bovine serum albumin as an additive
1Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, 70 Yuhua East Road, Shijiazhang 050018, P. R. China 2Tianjin Key Laboratory of Food-Biotechnology, Tianjin University of Commerce, Beichen District, Tianjin 300134, P. R. China 3, China
cjd007cn@163.com
Korean Journal of Chemical Engineering, February 2016, 33(2), 610-615(6), 10.1007/s11814-015-0190-z
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Abstract
Cross-linked enzyme aggregates from bovine pancreatic lipase were prepared by co-aggregation of lipase and BSA (Lipase-BSA-CLEAs). The main factors in the preparation of lipase-BSA-CLEAs were optimized. The highest activity recovery was around 75% under the condition of using 1% (v/v) glutaraldehyde as cross-linker and 0.05 g/L bovine serum albumin as feeder for 2 h cross linking. The optimum temperature for both lipase-CLEAs and lipase-BSA-CLEAs was measured as 60 oC, which is 10 oC higher than that of free lipase. Moreover, the lipase-BSA-CLEAs evidenced higher thermal stability and excellent reusability in comparison with the lipase-CLEAs. Lipase-BSA-CLEAs retained more than 75% of the initial activity after eight cycles of reuse, while lipase-CLEAs only retained 20% of its initial activity. Additionally, lipase-BSA-CLEAs showed more storage stability than free lipase and lipase-CLEAs. The high stability and recyclability of lipase-BSA-CLEAs make it efficient for different industrial applications.
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