Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems

被引:26
|
作者
Zhi, WB [1 ]
Song, JM [1 ]
Bi, JX [1 ]
Fan, OY [1 ]
机构
[1] Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China
关键词
alpha-amylase; aqueous two-phase systems; purification;
D O I
10.1007/s00449-004-0369-x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A study was made of the partition and purification of alpha-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 alpha-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 alpha-amylase was further improved to 2.0 of PF and 80% yield in a PEG3350-citrate ATPS with 4% sodium chloride.
引用
收藏
页码:3 / 7
页数:5
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