02542nas a2200241   4500008004100000022001400041245008900055210006900144260000900213300001600222490000800238520175100246100002501997700001502022700001702037700001702054700001902071700001902090700003202109700001802141700002002159856012102179       2023                        eng d  a0002-786300aCovalent organic framework cladding on peptide-amphiphile-based biomimetic catalysts0 aCovalent organic framework cladding on peptideamphiphilebased bi  cJUN   a12793-128010 v1453 a<p>
	Peptide-based biomimetic catalysts are promising materialsforefficient catalytic activity in various biochemical transformations.However, their lack of operational stability and fragile nature innon-aqueous media limit their practical applications. In this study,we have developed a cladding technique to stabilize biomimetic catalystswithin porous covalent organic framework (COF) scaffolds. This methodologyallows for the homogeneous distribution of peptide nanotubes insidethe COF (TpAzo and TpDPP) backbone, creating strong noncovalent interactionsthat prevent leaching. We synthesized two different peptide-amphiphiles,C10FFVK and C10FFVR, with lysine (K) and arginine(R) at the C-termini, respectively, which formed nanotubular morphologies.The C10FFVK peptide-amphiphile nanotubes exhibit enzyme-likebehavior and efficiently catalyze C-C bond cleavage in a buffermedium (pH 7.5). We produced nanotubular structures of TpAzo-C10FFVK and TpDPP-C10FFVK through COF claddingby using interfacial crystallization (IC). The peptide nanotubes encasedin the COF catalyze C-C bond cleavage in a buffer medium aswell as in different organic solvents (such as acetonitrile, acetone,and dichloromethane). The TpAzo-C10FFVK catalyst,being heterogeneous, is easily recoverable, enabling the reactionto be performed for multiple cycles. Additionally, the synthesis ofTpAzo-C10FFVK thin films facilitates catalysis inflow. As control, we synthesized another peptide-amphiphile, C10FFVR, which also forms tubular assemblies. By depositingTpAzo COF crystallites on C10FFVR nanotubes through IC,we produced TpAzo-C10FFVR nanotubular structuresthat expectedly did not show catalysis, suggesting the critical roleof the lysines in the TpAzo-C10FFVK.</p>
1 aMahato, Ashok, Kumar1 aPal, Sumit1 aDey, Kaushik1 aReja, Antara1 aPaul, Satyadip1 aShelke, Ankita1 aAjithkumar, Thalasseril, G.1 aDas, Dibyendu1 aBanerjee, Rahul  uhttps://library.ncl.res.in/content/covalent-organic-framework-cladding-peptide-amphiphile-based-biomimetic-catalysts02677nas a2200265   4500008004100000022001400041245008300055210006900138260000900207300001400216490000700230520184900237100001902086700001602105700001702121700002502138700001602163700001702179700001602196700001902212700002602231700002002257700002002277856011402297       2023                        eng d  a2041-652000aHierarchical covalent organic framework-foam for multi-enzyme tandem catalysis0 aHierarchical covalent organic frameworkfoam for multienzyme tand  cJUN   a6643-66530 v143 a<p>
	Covalent organic frameworks (COFs) are ideal host matrices for biomolecule immobilization and biocatalysis due to their high porosity, various functionalities, and structural robustness. However, the porosity of COFs is limited to the micropore dimension, which restricts the immobilization of enzymes with large volumes and obstructs substrate flow during enzyme catalysis. A hierarchical 3D nanostructure possessing micro-, meso-, and macroporosity could be a beneficial host matrix for such enzyme catalysis. In this study, we employed an in situ CO2 gas effervescence technique to induce disordered macropores in the ordered 2D COF nanostructure, synthesizing hierarchical TpAzo COF-foam. The resulting TpAzo foam matrix facilitates the immobilization of multiple enzymes with higher immobilization efficiency (approximately 1.5 to 4-fold) than the COF. The immobilized cellulolytic enzymes, namely beta-glucosidase (BGL), cellobiohydrolase (CBH), and endoglucanase (EG), remain active inside the TpAzo foam. The immobilized BGL exhibited activity in organic solvents and stability at room temperature (25 degrees C). The enzyme-immobilized TpAzo foam exhibited significant activity towards the hydrolysis of p-nitrophenyl-beta-d-glucopyranoside (BGL@TpAzo-foam: K-m and V-max = 23.5 +/- 3.5 mM and 497.7 +/- 28.0 mu M min(-1)) and carboxymethylcellulose (CBH@TpAzo-foam: K-m and V-max = 18.3 +/- 4.0 mg mL(-1) and 85.2 +/- 9.6 mu M min(-1) and EG@TpAzo-foam: K-m and V-max = 13.2 +/- 2.0 mg mL(-1) and 102.2 +/- 7.1 mu M min(-1)). Subsequently, the multi-enzyme immobilized TpAzo foams were utilized to perform a one-pot tandem conversion from carboxymethylcellulose (CMC) to glucose with high recyclability (10 cycles). This work opens up the possibility of synthesizing enzymes immobilized in TpAzo foam for tandem catalysis.</p>
1 aPaul, Satyadip1 aGupta, Mani1 aDey, Kaushik1 aMahato, Ashok, Kumar1 aBag, Saikat1 aTorris, Arun1 aGowd, Bhoje1 aSajid, Hasnain1 aAddicoat, Matthew, A.1 aDatta, Supratim1 aBanerjee, Rahul  uhttps://library.ncl.res.in/content/hierarchical-covalent-organic-framework-foam-multi-enzyme-tandem-catalysis