2011
DOI: 10.1016/j.chroma.2011.04.017
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A chromatography-focused bioprocess that eliminates soluble aggregation for bioactive production of a new antimicrobial peptide candidate

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Cited by 13 publications
(10 citation statements)
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References 40 publications
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“…Functional properties of bioactive peptides are determined by its unique three-dimensional (3D) structure, and further, secondary structure rather than tertiary structure is the dominant factor affecting the binding characteristics of the peptides (Alaiz et al 1992;Chan and Chen 2004;. Consequently, the purification criteria proposed so far have included MW or content of hydrophobic or cationic residues as the key factors (Li and Leong 2011;). …”
Section: Protein-derived Antioxidant Peptides (Bioactive Peptides)mentioning
confidence: 99%
“…Functional properties of bioactive peptides are determined by its unique three-dimensional (3D) structure, and further, secondary structure rather than tertiary structure is the dominant factor affecting the binding characteristics of the peptides (Alaiz et al 1992;Chan and Chen 2004;. Consequently, the purification criteria proposed so far have included MW or content of hydrophobic or cationic residues as the key factors (Li and Leong 2011;). …”
Section: Protein-derived Antioxidant Peptides (Bioactive Peptides)mentioning
confidence: 99%
“…The main peptide families of interest, defensins, and cathelicidins, are synthesized as precursor‐proteins that are proteolytically cleaved to produce mature peptides . These precursors protect host cells from the cytotoxic effects of the mature peptides, and fusion tags are used to mimic these precursors, preventing cytotoxicity, and successfully generating functional peptides.…”
Section: Tags For Functional Activitymentioning
confidence: 99%
“…This may be due to the large size of GST (28 kDa), especially in relation to the small antimicrobial peptides. MBP has been used for the production of Human β‐defensin 25 (hBD25) and Human β‐defensin 28 (hBD28), but both required refolding steps to recover fusion protein from aggregates in purification …”
Section: Tags For Functional Activitymentioning
confidence: 99%
“…Most of the carrier proteins are then cleaved and separated from AMPs. The available carrier proteins and cleavable linkers have been reviewed by Li et al (Li 2011). Deng et al reviewed different types of cell factories used to produce AMPs, including Escherichia coli, Bacillus subtilis, Pichia pastoris and Saccharomyces cerevisae (Deng et al 2017).…”
Section: Introductionmentioning
confidence: 99%