Binding Peptide-Guided Immobilization of Lipases with Significantly Improved Catalytic Performance Using Escherichia coli BL21(DE3) Biofilms as a Platform was written by Dong, Hao;Zhang, Wenxue;Xuan, Qize;Zhou, Yao;Zhou, Shengmin;Huang, Jiaofang;Wang, Ping. And the article was included in ACS Applied Materials & Interfaces in 2021.HPLC of Formula: 84-61-7 This article mentions the following:
Developing novel immobilization methods to maximize the catalytic performance of enzymes has been a permanent pursuit of scientific researchers. Engineered Escherichia coli biofilms have attracted great concern as surface display platforms for enzyme immobilization. However, current biol. conjugation methods, such as the SpyTag/SpyCatcher tagging pair, that immobilize enzymes onto E. coli biofilms seriously hamper enzymic performance. Through phage display screening of lipase-binding peptides (LBPs) and co-expression of CsgB (nucleation protein of curli nanofibers) and LBP2-modified CsgA (CsgALBP2, major structural subunit of curli nanofibers) proteins, we developed E. coli BL21::铻朇sgA-CsgB-CsgALBP2 (LBP2-functionalized) biofilms as surface display platforms to maximize the catalytic performance of lipase (Lip181). After immobilization onto LBP2-functionalized biofilm materials, Lip181 showed increased thermostability, pH, and storage stability. Surprisingly, the relative activity of immobilized Lip181 increased from 8.43 to 11.33 U/mg through this immobilization strategy. Furthermore, the highest loading of lipase on LBP2-functionalized biofilm materials reached up to 27.90 mg/g of wet biofilm materials, equivalent to 210.49 mg/g of dry biofilm materials, revealing their potential as a surface with high enzyme loading capacity. Addnl., immobilized Lip181 was used to hydrolyze phthalic acid esters, and the hydrolysis rate against di-Bu phthalate was up to 100%. Thus, LBP2-mediated immobilization of lipases was demonstrated to be far more advantageous than the traditional SpyTag/SpyCatcher strategy in maximizing enzymic performance, thereby providing a better alternative for enzyme immobilization onto E. coli biofilms. In the experiment, the researchers used many compounds, for example, Dicyclohexyl phthalate (cas: 84-61-7HPLC of Formula: 84-61-7).
Dicyclohexyl phthalate (cas: 84-61-7) belongs to esters. Esters typically have a pleasant smell; those of low molecular weight are commonly used as fragrances and are found in essential oils and pheromones. Esterification is the general name for a chemical reaction in which two reactants (typically an alcohol and an acid) form an ester as the reaction product. Esters are common in organic chemistry and biological materials.HPLC of Formula: 84-61-7
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics