Solid‐Phase Lipase‐CuNPs Biohybrids as Catalysts for One‐Pot Parallel Synthesis of 2,3,4‐Triacetyl‐D‐Gluconic Acid

Abstract

Solid-phase lipase/metal nanobiohybrids, generated by growth of copper nanoparticles on enzyme matrixes immobilized on graphene, were used as heterogeneous catalysts with dualactivity for the regioselective production of 2,3,4-triacetyl-Dgluconic acid from α-peracetylated-glucose in a one-pot parallel process combining a lipase-mediated regioselective hydrolytic monodeprotection with a metal-catalyzed oxidation in aqueous media. A novel synthetic strategy, based on the in situ fabrication of Cu nanoparticles induced by lipase molecules specifically immobilized on a multi-layer graphene material by interfacial adsorption fixing them in the active open conformation, has been described. Thermomyces lanuginosus lipase was firstly used to prepare the functionalized multi-layer graphene from graphite as a biographene preparation (Biographene, BIOG), support used to successfully immobilize Candida rugosa lipase (CRL). This immobilized form BIOG-CRL was further used to create successful active bifunctional enzyme-metal nanoarchitectures. Two different Cu-lipase hybrids were synthesised, where Cu species and nanoparticles size were different depending on the methodology. Regioselectivity and stability of the hybrids were evaluated successfully in the production of monosaccharide building blocks, besides the robustness of the hybrids in recyclability experiments. These findings highlight the potential of these solid-phase nanoarchitectures as useful tools in the synthesis of complex glycoderivatives for use in food, medicine, and cosmetics.

Preparation of Dual‐activity Enzyme‐metal‐nanoparticles Conjugate Catalysts for Cascade Processes

“…Finally, one of the most critical aspects in achieving optimum stability and enzymatic activity has been the innovative creation of nanobiohybrids on solid-phase (Figure 5). [31,34] The site-specific immobilization of enzymes provides for the most stable and active form of these biocatalysts. Thus, the prior experimental conditions for metal nanoparticle formation can be applied utilizing this solid-phase enzyme.…”

“…[31,34] This property was recently expanded to other enzymes, including co-immobilization of two distinct enzymes on the same solid material. [31,34] Enzymatic activity was mostly preserved in all circumstances, such as when creating Cu nanoparticles or even Pd nanoparticles.…”

“…[31] In a second example of the applicability of this dual-activity catalysts in carbohydrate chemistry, a Graphene-Candida rugosa lipase (CRL)-CuNPs was prepared. [34] A one-pot parallel process combining a lipase-mediated regioselective hydrolytic monodeprotection with a metal-catalyzed oxidation in aqueous media was performed to synthesize 2,3,4-triacetyl-D-gluconic acid from αperacetylated-glucose. As in the first example, the enzyme was extremely selective for regiodeprotection at C-6 position of peracetylated glucose.…”

“…Lipase immobilized fixing the open conformation on graphene derivative displayed the maximum activity, which is retained after the nanobiohybrid creation. [31,34] This property was recently expanded to other enzymes, including co-immobilization of two distinct enzymes on the same solid material. [31,34] Enzymatic activity was mostly preserved in all circumstances, such as when creating Cu nanoparticles or even Pd nanoparticles.…”

“…[26][27] Some of these results are the most relevant in the literature in the particular catalytic process, demonstrating the advantages to use nanotechnology vs bulk materials, besides the simple synthetic approach of them. The conservation of both activities, producing bifunctional (enzyme and metal) catalysts have been recently successfully used in complex chemical routes by cascade processes in very sustainable conditions, [28][29][30][31][32][33][34][35][36] and some of them will be discussed in this article (Figure 1).…”