Multienzyme Cellulose Films as Sustainable and Self-Degradable Hydrogen Peroxide-Producing Material

Autor(es)

Califano, Davide ^[1] ; Kadowaki, Marco A. S. ^[2] ; Calabrese, Vincenzo ^[1] ; Prade, Rolf Alexander ^{[3, 4]} ; Mattia, Davide ^[5] ; Edler, Karen J. ^[1] ; Polikarpov, Igor ^[2] ; Scott, Janet L. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Bath, Dept Chem, Bath BA2 7AY, Avon - England

^[2] Univ Sao Paulo, Sao Carlos Inst Phys, BR-13566590 Sao Carlos, SP - Brazil

^[3] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 - USA

^[4] Oklahoma State Univ, Dept Biochem & Mol Biol, Stillwater, OK 74078 - USA

^[5] Univ Bath, Dept Chem Engn, Bath BA2 7AY, Avon - England

• Tipo de documento: Artigo Científico
• Fonte: Biomacromolecules; v. 21, n. 12, p. 5315-5322, DEC 2020.
• Citações Web of Science: 0

Resumo

The use of hydrogen peroxide-releasing enzymes as a component to produce alternative and sustainable antimicrobial materials has aroused interest in the scientific community. However, the preparation of such materials requires an effective enzyme binding method that often involves the use of expensive and toxic chemicals. Here, we describe the development of an enzyme-based hydrogen peroxide-producing regenerated cellulose film (RCF) in which a cellobiohydrolase (TrCBHI) and a cellobiose dehydrogenase (MtCDHA) were efficiently adsorbed, 90.38 +/- 2.2 and 82.40 +/- 5.7%, respectively, without making use of cross-linkers. The enzyme adsorption kinetics and binding isotherm experiments showed high affinity of the proteins possessing cellulose-binding modules for RCF, suggesting that binding on regenerated cellulose via specific interactions can be an alternative method for enzyme immobilization. Resistance to compression and porosity at a micrometer scale were found to be tunable by changing cellulose concentration prior to film regeneration. The self-degradation process, triggered by stacking TrCBHI and MtCDHA (previously immobilized onto separate RCF), produced 0.15 nmol/min.cm(2) of H2O2. Moreover, the production of H2O2 was sustained for at least 24 h reaching a concentration of similar to 2 mM. The activity of MtCDHA immobilized on RCF was not affected by reuse for at least 3 days (1 cycle/day), suggesting that no significant enzyme leakage occurred in that timeframe. In the material herein designed, cellulose (regenerated from a 1-ethyl-3-methylimidazolium acetate/dimethyl sulfoxide (DMSO) solution) serves both as support and substrate for the immobilized enzymes. The sequential reaction led to the production of H2O2 at a micromolar-millimolar level revealing the potential use of the material as a self-degradable antimicrobial agent. (AU)

• Processo FAPESP: 11/20505-4 - Duas classes importantes de glicosil hidrolases: estudos funcionais e análise estrutural
• Beneficiário: Marco Antonio Seiki Kadowaki
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado