| Autor: |
Santiago-Arcos J; Heterogeneous Biocatalysis Laboratory, CIC biomaGUNE, Edificio Empresarial 'C', Paseo de Miramón 182, 20009 Donostia, Spain., Velasco-Lozano S; Heterogeneous Biocatalysis Laboratory, CIC biomaGUNE, Edificio Empresarial 'C', Paseo de Miramón 182, 20009 Donostia, Spain.; Instituto de Síntesis Química y Catálisis Homogénea (ISQCH-CSIC), Universidad de Zaragoza, C/ Pedro Cerbuna, 12, 50009 Zaragoza, Spain.; Aragonese Foundation for Research and Development (ARAID), 50018 Zaragoza, Spain., López-Gallego F; Heterogeneous Biocatalysis Laboratory, CIC biomaGUNE, Edificio Empresarial 'C', Paseo de Miramón 182, 20009 Donostia, Spain.; IKERBASQUE, Basque Foundation for Science, 48009 Bilbao, Spain. |
| Abstrakt: |
Immobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide variety of different enzymes. This support is based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties that allow a fast and irreversible immobilization of enzymes, enhancing the thermostability of most of the heterogeneous biocatalysts (up to 21-fold higher than the soluble one). Furthermore, this trifunctional support serves to efficiently coimmobilize a multienzyme system composed of an alcohol dehydrogenase, a reduced nicotinamide adenine dinucleotide (NADH) oxidase, and a catalase. The confined multienzymatic system demonstrates higher performance than its free counterpart, achieving a total turnover number (TTN) of 1 × 10 5 during five batch consecutive cycles. We envision this solid material as a platform for coimmobilizing multienzyme systems with enhanced properties to catalyze stepwise biotransformations. |
