Molecular modification, expression and purification of new subtype antioxidant peptide from Pinctada fucata by recombinant Escherichia coli to improve antioxidant-activity

Wu, Yanyan; Ma, Yun‐Bao; Li, Laihao

doi:10.1007/s13197-018-3365-x

Cited by 2 publications

(1 citation statement)

References 36 publications

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“…However, glycosylation performed by S. cerevisiae is sometimes unfavorable for the production of mammalian proteins as O-linked oligosaccharides often include mannose, whereas higher eukaryotic proteins produce sialylated O-linked chains [ 78 , 79 ]. In addition, the yeast over-glycosylates N-linked sites, which leads to reduced activity and receptor binding and may trigger an immune reaction [ 80 ]. Marketed items that are manufactured with S. cerevisiae include insulin, hepatitis B surface antigen, urate oxidase, glucagons, granulocyte-macrophage colony-stimulating factor (GM-CSF), hirudin, and platelet-derived growth factor [ 81 , 82 ].…”

Section: Host Strains For the Overexpression Of Target Proteinsmentioning

confidence: 99%

Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds

Lee

Park

2020

Antibiotics

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Bacteria can produce recombinant proteins quickly and cost effectively. However, their physiological properties limit their use for the production of proteins in their native form, especially polypeptides that are subjected to major post-translational modifications. Proteins that rely on disulfide bridges for their stability are difficult to produce in Escherichia coli. The bacterium offers the least costly, simplest, and fastest method for protein production. However, it is difficult to produce proteins with a very large size. Saccharomyces cerevisiae and Pichia pastoris are the most commonly used yeast species for protein production. At a low expense, yeasts can offer high protein yields, generate proteins with a molecular weight greater than 50 kDa, extract signal sequences, and glycosylate proteins. Both eukaryotic and prokaryotic species maintain reducing conditions in the cytoplasm. Hence, the formation of disulfide bonds is inhibited. These bonds are formed in eukaryotic cells during the export cycle, under the oxidizing conditions of the endoplasmic reticulum. Bacteria do not have an advanced subcellular space, but in the oxidizing periplasm, they exhibit both export systems and enzymatic activities directed at the formation and quality of disulfide bonds. Here, we discuss current techniques used to target eukaryotic and prokaryotic species for the generation of correctly folded proteins with disulfide bonds.

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Section: Host Strains For the Overexpression Of Target Proteinsmentioning

confidence: 99%

Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds

Lee

Park

2020

Antibiotics

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Recombinant Active Peptides and their Therapeutic Functions

Ajingi

Rukying

Aroonsri

et al. 2022

CPB

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: Recombinant active peptides are utilized as diagnostic and biotherapeutics in various maladies and as bacterial growth inhibitors in the food industry. This consequently stimulated the need for recombinant peptides' production, which resulted in about 19 approved biotech peptides of 1-100 amino acids commercially available. While most peptides have been produced by chemical synthesis, the production of lengthy and complicated peptides comprising natural amino acids has been problematic with low quantity. Recombinant peptide production has become very vital, cost-effective, simple, environmentally friendly with satisfactory yields. Several reviews have focused on discussing expression systems, advantages, disadvantages, and alternatives strategies. Additionally, the information on the antimicrobial activities and other functions of multiple recombinant peptides is challenging to access and is scattered in literature apart from the food and drug administration (FDA) approved ones. From the reports that come to our knowledge, there is no existing review that offers substantial information on recombinant active peptides developed by researchers and their functions. This review provides an overview of some successfully produced recombinant active peptides of ≤100 amino acids by focusing on their antibacterial, antifungal, antiviral, anticancer, antioxidant, antimalarial, and immune-modulatory functions. It also elucidates their modes of expression that could be adopted and applied in future investigations. We expect that the knowledge available in this review would help researchers involved in recombinant active peptide development for therapeutic uses and other applications.

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Molecular modification, expression and purification of new subtype antioxidant peptide from Pinctada fucata by recombinant Escherichia coli to improve antioxidant-activity

Cited by 2 publications

References 36 publications

Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds

Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds

Recombinant Active Peptides and their Therapeutic Functions

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