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

Wenbo Zhi, Jiangnan Song, Jingxiu Bi, Fan Ouyang

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

A study was made of the partition and purification of α-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 α-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 α-amylase was further improved to 2.0 of PF and 80% yield in a PEG3350-citrate ATPS with 4% sodium chloride.

Original languageEnglish (US)
Pages (from-to)3-7
Number of pages5
JournalBioprocess and Biosystems Engineering
Volume27
Issue number1
DOIs
StatePublished - Dec 1 2004
Externally publishedYes

Fingerprint

Amylases
Bacilli
Bacillus subtilis
Citric Acid
Purification
Sodium Chloride
Salts
Sodium chloride
Polyethylene glycols
Molecular Weight
Molecular weight
Proteins

Keywords

  • Aqueous two-phase systems
  • Purification
  • α-Amylase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems. / Zhi, Wenbo; Song, Jiangnan; Bi, Jingxiu; Ouyang, Fan.

In: Bioprocess and Biosystems Engineering, Vol. 27, No. 1, 01.12.2004, p. 3-7.

Research output: Contribution to journalArticle

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