A novel protein fusion partner, carbohydrate-binding module family 66, to enhance heterologous protein expression in Escherichia coli was written by Ko, Hyunjun;Kang, Minsik;Kim, Mi-Jin;Yi, Jiyeon;Kang, Jin;Bae, Jung-Hoon;Sohn, Jung-Hoon;Sung, Bong Hyun. And the article was included in Microbial Cell Factories in 2021.Application of 367-93-1 The following contents are mentioned in the article:
Proteins with novel functions or advanced activities developed by various protein engineering techniques must have sufficient solubility to retain their bioactivity. However, inactive protein aggregates are frequently produced during heterologous protein expression in Escherichia coli. To prevent the formation of inclusion bodies, fusion tag technol. has been commonly employed, owing to its good performance in soluble expression of target proteins, ease of application, and purification feasibility. Thus, researchers have continuously developed novel fusion tags to expand the expression capacity of high-value proteins in E. coli. A novel fusion tag comprising carbohydrate-binding module 66 (CBM66) was developed for the soluble expression of heterologous proteins in E. coli. The target protein solubilization capacity of the CBM66 tag was verified using seven proteins that are poorly expressed or form inclusion bodies in E. coli: four human-derived signaling polypeptides and three microbial enzymes. Compared to native proteins, CBM66-fused proteins exhibited improved solubility and high production titer. The protein-solubilizing effect of the CBM66 tag was compared with that of two com. tags, maltose-binding protein and glutathione-S-transferase, using poly(ethylene terephthalate) hydrolase (PETase) as a model protein; CBM66 fusion resulted in a 3.7-fold higher expression amount of soluble PETase (approx. 370 mg/L) compared to fusion with the other com. tags. The intact PETase was purified from the fusion protein upon serial treatment with enterokinase and affinity chromatog. using levan-agarose resin. The bioactivity of the three proteins assessed was maintained even when the CBM66 tag was fused. The use of the CBM66 tag to improve soluble protein expression facilitates the easy and economic production of high-value proteins in E. coli. This study involved multiple reactions and reactants, such as (2R,3R,4S,5R,6S)-2-(Hydroxymethyl)-6-(isopropylthio)tetrahydro-2H-pyran-3,4,5-triol (cas: 367-93-1Application of 367-93-1).
(2R,3R,4S,5R,6S)-2-(Hydroxymethyl)-6-(isopropylthio)tetrahydro-2H-pyran-3,4,5-triol (cas: 367-93-1) belongs to alcohols. Because alcohols are easily synthesized and easily transformed into other compounds, they serve as important intermediates in organic synthesis. Grignard and organolithium reagents are powerful tools for organic synthesis, and the most common products of their reactions are alcohols.Application of 367-93-1
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts