Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/46418
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Type: | Journal article |
Title: | Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems |
Other Titles: | Partial purification of alpha-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems |
Author: | Zhi, W. Song, J. Bi, J. Ouyang, F. |
Citation: | Bioprocess and Biosystems Engineering: bioreactors, upstream and downstream processes, measurement and control, 2004; 27(1):3-7 |
Publisher: | Springer |
Issue Date: | 2004 |
ISSN: | 1615-7591 1615-7605 |
Statement of Responsibility: | Wenbo Zhi, Jiangnan Song, Jingxiu Bi and Fan Ouyang |
Abstract: | A study was made of the partition and purification of -amylase from a culture supernatant of Bacillus subtilis in the polyethylene glycol (PEG)—citrate aqueous two-phase system (ATPS). Factors that influenced the partition of the protein in this system, including the molecular weight of the PEG, the tie line length of ATPS, the pH value and the sodium chloride concentration, were investigated. Purification of -amylase was attained with a purification factor (PF) of 1.8 and 90% yield at pH 6.0 in a PEG1000-citrate ATPS with short tie line length. By utilizing the salt-out effect of neutral salt, the purification of -amylase was further improved to 2.0 of PF and 80% yield in a PEG3350-citrate ATPS with 4% sodium chloride. |
Keywords: | α-Amylase Aqueous two-phase systems Purification |
Description: | The original publication can be found at www.springerlink.com |
Provenance: | Published online: 13 August 2004 |
Rights: | © Springer |
DOI: | 10.1007/s00449-004-0369-x |
Published version: | http://dx.doi.org/10.1007/s00449-004-0369-x |
Appears in Collections: | Aurora harvest 6 Chemical Engineering publications |
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hdl_46418.pdf | 290.74 kB | Author's post-print | View/Open |
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