Coupling and Regulation of Porous Carriers Using Plasma and Amination to Improve the Catalytic Performance of Glucose Oxidase and Catalase

Abstract

Multiple enzyme systems are being increasingly used for their high-efficiency and co-immobilization is a key technology to lower the cost and improve the stability of enzymes. In this study, poly glycidyl methacrylate (PGMA) spheres were synthesized using suspension polymerization, and were used as a support to co-immobilize glucose oxidase (GOx) and catalase (CAT). Surface modification was carried out via a combination of plasma and amination to promote the properties of the catalyzer. The co-immobilized enzymes showed a more extensive range of optimum pH and temperature from 5.5 to 7.5 and 25 to 40 • C, respectively, compared to free enzymes. Furthermore, the maximum activity and protein adsorption quantity of the co-immobilized enzymes reached 25.98 U/g and 6.07 mg/g, respectively. The enzymatic activity of the co-immobilized enzymes was maintained at ∼70% after storage for 5 days and at 82% after three consecutive cycles, indicating that the immobilized material could be applied industrially.

Enzyme production ofd-gluconic acid and glucose oxidase: successful tales of cascade reactions

“…278 Recently, polyglycidyl methacrylate spheres were utilized to coimmobilize glucose oxidase and catalase. 279 The support was activated with a combination of amination and plasma. Immobilization increases the optimal pH (from 5.5 to 7.5) and temperature (from 25°C to 40°C) so that 82% of the initial activity was maintained after three glucose oxidation batches; although this value was considered good by the authors, it is not high enough for industrial implementation of the biocatalyst.…”

“…Immobilization increases the optimal pH (from 5.5 to 7.5) and temperature (from 25°C to 40°C) so that 82% of the initial activity was maintained after three glucose oxidation batches; although this value was considered good by the authors, it is not high enough for industrial implementation of the biocatalyst. 279 Crosslinked enzyme aggregates [280][281][282] have been also utilized in some instances to co-immobilize catalase and glucose oxidase (Fig. 11).…”

Immobilization of Multi-Enzymes on Support Materials for Efficient Biocatalysis

“…Wang's group prepared polystyrene particles to co-immobilize formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), alcohol dehydrogenase (ADH), glutamate dehydrogenase (GDH), and cofactor NADH/NAD + , which achieved efficient cofactor regeneration for the synthesis of methanol from CO 2 (El-Zahab et al, 2008 ). Similarly, polyglycidyl methacrylate (PGMA) spheres were also used for the co-immobilization of GOx and catalase for the preparation of gluconic acid from glucose (Liao et al, 2019 ). Zhang's group fabricated a polyurethane hollow nanofiber via a co-axial electrospinning technique, which could be used for the co-immobilization of 3a-hydroxysteroid dehydrogenase (3a-HSD), diaphorase (DP), and NADH (Ji et al, 2014 ).…”

Alcalase Microarray Base on Metal Ion Modified Hollow Mesoporous Silica Spheres as a Sustainable and Efficient Catalysis Platform for Proteolysis

“…The insufficient stability of enzyme under processing conditions is the major barrier for enzyme industrial application, high temperature, or inappropriate pH value would cause the reversible or irreversible denaturation of enzyme, which would cause the losses of enzyme activity (Orfanakis et al, 2018;Liao et al, 2019). Thus, in order to check whether the prepared biocatalyst was suitable under catalytic conditions, the effects of temperature and pH value on free alcalase and alcalase@HMSS-NH 2 -Fe 3+ were further evaluated.…”