Advances in the One-Step Approach of Polymeric Materials Using Enzymatic Techniques

Abstract

The formulation in which biochemical enzymes are administered in polymer science plays a key role in retaining their catalytic activity. The one-step synthesis of polymers with highly sequence-controlled enzymes is a strategy employed to provide enzymes with higher catalytic activity and thermostability in material sustainability. Enzyme-catalyzed chain growth polymerization reactions using activated monomers, protein-polymer complexation techniques, covalent and non-covalent interaction, and electrostatic interactions can provide means to develop formulations that maintain the stability of the enzyme during complex material processes. Multifarious applications of catalytic enzymes are usually attributed to their efficiency, pH, and temperature, thus, progressing with a critical structure-controlled synthesis of polymer materials. Due to the obvious economics of manufacturing and environmental sustainability, the green synthesis of enzyme-catalyzed materials has attracted significant interest. Several enzymes from microorganisms and plants via enzyme-mediated material synthesis have provided a viable alternative for the appropriate synthesis of polymers, effectively utilizing the one-step approach. This review analyzes more and deeper strategies and material technologies widely used in multi-enzyme cascade platforms for engineering polymer materials, as well as their potential industrial applications, to provide an update on current trends and gaps in the one-step synthesis of materials using catalytic enzymes.

Keywords: application; enzymatic approach; one-step synthesis; polymer materials.

Figure 1

Phase change materials to improve thermal conductivity prepared in a one-step synthesis. (A) Illustration of the silica aerogel-based composite PCMs’ schematic synthesis, (B) a scanning electron microscope image of the silica aerogel, and (C) a transmission electron microscope image, consisting of primary nanoparticles (approximately 30 nm) and aggregated nanoparticles in a linked, three-dimensional porous structure. (D) TEM mapping images of the silica aerogel consisting of evenly distributed C, N, O, and Si elements [22], with permission from Elsevier, copyright (2020).

Figure 2

(A) Typical enzyme-catalyzed reactions, comparing the natural catalytic active site and triad of esterases and the artificial enzyme mimic integrated into the polystyrene Merrifield resin, demonstrating various catalytic sites and hydrophobic tailoring enabled by functionalized resins [51], with permission from Elsevier, copyright (2017). (B) A representation of the heating–centrifuging and cooling–oscillation cycle for the recycling of pNIPAM/DNAzyme microgels [46] with permission from Wiley periodicals Inc. (2022).

Figure 3

A multi-enzyme cascade development cycle that has been analyzed and implemented. Whereas a wider variety of biocatalysts are now readily available, both in vitro and in vivo de novo enzyme pathway development is becoming easier using a biocatalytic retrosynthetic strategy [103], with permission from the American Chemical Society, copyright (2017).

Figure 4

Comparison of (i) in vitro reaction and (ii) in vivo reaction with (iii) hybrid cascade reactions, utilizing potent and selective biocatalysts cat i–iii to develop product D from starting material A. Several parameters such as the availability of genetic sequences and recombinant enzymes, the need for cofactors, the absorption and release of substrates and products, and the metabolic stability influence which of these three possibilities is best for a given application [103], with permission from the American Chemical Society, copyright (2017).

Figure 5

(A) Illustrating a general cascaded reaction mechanism and its operation. The figure made in Biorender.com. (B) A representation of the recycling use of the microgels through heating/centrifuging and cooling/oscillation cycles, as well as DNA/GOx cascaded catalyzed oxidation of glucose/ABTS^2-. After the reaction, the microgels were removed from the reaction mixture using a heating–centrifuging technique and recycled by catalyzing a new DNA substrate following a cooling–oscillation dispersion procedure [46], with permission from Wiley periodicals Inc. (2018). (C) in the presence of an NIR laser, VOxBG catalyzes the conversion of starch into glucose (step I). In the presence of H₂O₂, GOx catalyzes the oxidation of glucose to produce H₂O₂, while VOxBG acting as HRP catalyzes the oxidation of TMB to produce colored compounds which changes in response to the different pH values (step II), (D) the photolithography process is illustrated, in a polyacrylamide hydrogel, starch and VOxBG are incorporated, (E) various geometric designs are created by photolithographing the hydrogel [125], with permission from the American Chemical Society, copyright (2020).

Figure 6

Schematic illustrations of the one-step nano-enzyme synthesis. (A) A hydrolytic enzyme with an oxyanion hole and a catalytic triad. In a Ser–His–Asp motif, the carboxyl group of aspartate forms a hydrogen bond with the imidazole domains of histidine. The hydroxy group of serine that is close by is subsequently deprotonated by the imidazole group to produce a nucleophile, (B) using nanoprecipitation in water to generate polystyrene-supported catalysts with urea and ACT groups. Here, a facile one-step method for synthesizing polystyrene-supported catalytic systems with integrated and tailored ACTs, urea groups, and hydrophobic environments is devised [136], with permission from Elsevier, copyright (2022), (C) fabrication of nanozyme-enzyme multi-catalyst system, reproduced from reference [137], (D,E) illustration of the synthesis of Cu/Cys nanozyme with laccase-like activity, reproduced from reference [134], (F) RAFT-Mediated emulsion polymerization in water followed by TDMT and ultrasonic cutting to generate multifunctional nanoworms and nanorods [138], with permission from the American Chemical Society copyright (2014).

Figure 7

Fabrication of highly efficient combi-metal organic frameworks [139], adapted with permission from Elsevier, copyright (2018).

Figure 8

(A) Illustration of the of the in situ PdCu/CALB CLEA fabrication process. (B) HAADF-STEM picture of the hybrid catalyst composed of PdCu and CALB CLEAs. (C) An elemental map of Pd, Cu, N, and S that corresponds to (D) CALB and CALB CLEAs FT-IR spectra and (E) powder XRD patterns [141], with permission from Elsevier, copyright (2023).

Figure 8

(A) Illustration of the of the in situ PdCu/CALB CLEA fabrication process. (B) HAADF-STEM picture of the hybrid catalyst composed of PdCu and CALB CLEAs. (C) An elemental map of Pd, Cu, N, and S that corresponds to (D) CALB and CALB CLEAs FT-IR spectra and (E) powder XRD patterns [141], with permission from Elsevier, copyright (2023).

Figure 9

Hybrid DNA/protein cage architecture. (A) Addition of ssDNA handles to a site-specific reactive residue on an aldolase homotrimer (ald3) protein building block (B) self-assembly of three complementary handles and a triangular base for the protein from four distinct DNA strands and (C) by annealing the protein–DNA conjugate with a triangular base, a tetrahedral cage composed of both protein and DNA molecules is constructed. The cage’s proportions can be adjusted by altering the lengths of the DNA strands in the triangle-shaped base [147], with permission from the American Chemical Society, copyright (2019).

Figure 10

Synthesis of metal nano-biohybrids using enzyme–polymer conjugates. Illustrating the attempted prevention of mutual deactivation of the coupled enzyme and metal entities through poisoning effects in the nano-biohybrid synthesis by using polymer additives in the structure of the enzyme–metal nano-biohybrids [152], with permission from Wiley periodicals Inc., copyright (2022).

Figure 11

(A) Structural information of three heptapeptides ((i) Ac-IHIHIQI-CONH₂, (ii) Ac-IHIHIYI-CONH₂, (iii) Ac-IHVHLQI-CONH₂)). (B) Schematic illustration showing the design of Zn-heptapeptide bionanozymes for hydrolysis of p-nitrophenyl esters and degradation of DEHP [153], with permission from Elsevier, copyright (2022). (C,D) SEM with difference magnifications, (E) TEM, and (F) HR-TEM images of BSA-Mn₃(PO₄)₂⋅3H₂O hybrid nanoflower (MnPNF) [154], with permission from Elsevier, copyright (2021).

Figure 12

(A) Schematic representation of the Cu ion grafted by DA coating on the SLM-fabricated Ti6Al4V scaffold, which gave the scaffold the ability to stimulate angiogenesis and osteogenesis by releasing Cu ions. (B) Differential appearance of printed structures before and after PDA/Cu coating showing the changes in scaffold’s appearance [165], with permission from MDPI, Basel, copyright (2022).