2022
DOI: 10.1016/j.foodchem.2021.131543
|View full text |Cite
|
Sign up to set email alerts
|

Combination of aqueous two-phase flotation and inverse transition cycling: Strategies for separation and purification of recombinant β-glucosidase from cell lysis solution

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
4
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
6

Relationship

1
5

Authors

Journals

citations
Cited by 12 publications
(4 citation statements)
references
References 31 publications
0
4
0
Order By: Relevance
“…[59,60] Inverse conversion cycling (ITC) is a technique to purify recombinant proteins based on the thermo-responsive properties of elastin-like peptides (ELPs), where ELP-tagged proteins can be precipitated from fermentation broth when ambient temperature is higher than the phase transition temperature (Tt), resulting in higher purity proteins. Han et al [61] established a method combined ATPF with ITC for efficient purification of recombinant protein β-glucosidase (GLEGB) dependent on graphene-binding tag (GB) and ELP tag from cell lysates. GLEGB is preferentially adsorbed on the nitrogen bubble interface due to the hydrophobicity of GB, entered the top phase of ATPF, and then based on the thermo-responsive properties of the ELP tag, with a final purification ploidy of 24.26 ± 0.22 and the protein remaining structurally stable after six cycles of purification.…”
Section: Dual Aqueous Phase Flotation (Atpf) Combined With Inverse Tr...mentioning
confidence: 99%
See 1 more Smart Citation
“…[59,60] Inverse conversion cycling (ITC) is a technique to purify recombinant proteins based on the thermo-responsive properties of elastin-like peptides (ELPs), where ELP-tagged proteins can be precipitated from fermentation broth when ambient temperature is higher than the phase transition temperature (Tt), resulting in higher purity proteins. Han et al [61] established a method combined ATPF with ITC for efficient purification of recombinant protein β-glucosidase (GLEGB) dependent on graphene-binding tag (GB) and ELP tag from cell lysates. GLEGB is preferentially adsorbed on the nitrogen bubble interface due to the hydrophobicity of GB, entered the top phase of ATPF, and then based on the thermo-responsive properties of the ELP tag, with a final purification ploidy of 24.26 ± 0.22 and the protein remaining structurally stable after six cycles of purification.…”
Section: Dual Aqueous Phase Flotation (Atpf) Combined With Inverse Tr...mentioning
confidence: 99%
“…Han et al. [ 61 ] established a method combined ATPF with ITC for efficient purification of recombinant protein β‐glucosidase (GLEGB) dependent on graphene‐binding tag (GB) and ELP tag from cell lysates. GLEGB is preferentially adsorbed on the nitrogen bubble interface due to the hydrophobicity of GB, entered the top phase of ATPF, and then based on the thermo‐responsive properties of the ELP tag, with a final purification ploidy of 24.26 ± 0.22 and the protein remaining structurally stable after six cycles of purification.…”
Section: Biosynthesis Technology Of Peptide Drugsmentioning
confidence: 99%
“…The recovery of WSP is regarded as the inaugural phase in the comprehensive resource recovery process from SWW . At present, foam separation is often considered the most cost-effective strategy for protein recovery . Unfortunately, WSP exhibits poor interfacial stability and tends to aggregate into insoluble particles.…”
Section: Introductionmentioning
confidence: 99%
“…27 At present, foam separation is often considered the most cost-effective strategy for protein recovery. 28 Unfortunately, WSP exhibits poor interfacial stability and tends to aggregate into insoluble particles. Its foams are also prone to coarsening and rupturing, leading to a lower recovery rate of WSP.…”
Section: ■ Introductionmentioning
confidence: 99%