title: Expression of a collagen-binding domain fusion protein: effect of amino acid supplementation, inducer type, and culture conditions.
abstract: Collagen binding domain fusion proteins are of significant importance because of their potential as therapeutic biomaterials. In this paper, we investigate the production of such therapeutic proteins via fermentation of Escherichia coli on both an undefined medium and a defined medium. Defined media with amino acid supplementation provided higher amounts of therapeutic protein than undefined media with no supplementation. Additionally, utilizing lactose instead of isopropyl-β-d-thio-galactoside (IPTG) for induction and extending batch time yielded higher amounts of the model therapeutic.
authors: Boston Mountain Biotech LLC, Fayetteville, AR, 72701.
authors: McKinzie
authors: M
authors: Fruchtl
authors: Joshua
authors: J
authors: Sakon
authors: Robert
authors: R
authors: Beitle
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D001709:Biotechnology; D003094:Collagen / Q000378:metabolism*; D003470:Culture Media / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D007544:Isopropyl Thiogalactoside; D007785:Lactose / Q000378:metabolism; D010957:Plasmids; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D003470:Culture Media; D011993:Recombinant Fusion Proteins; D007544:Isopropyl Thiogalactoside; D003094:Collagen; D005947:Glucose; D007785:Lactose
keywords: collagen binding domain fusions; fermentation; relative cytoplasmic dilution rate; total synthesis/accumulation time