Nanofibrillated Cellulose-Enzyme Assemblies for Enhanced Biotransformations with In Situ Cofactor Regeneration

Guoying Dai, William Tai Yin Tze, Benjiamin Frigo-Vaz, Natalia Calixto Mancipe, Han Seung Yang, Marcia Cristina Branciforti, Ping Wang

Research output: Contribution to journalArticlepeer-review

Abstract

We report herein the use of nanofibrillated cellulose (NFC) for development of enzyme assemblies in an oriented manner for biotransformation with in situ cofactor regeneration. This is achieved by developing fusion protein enzymes with cellulose-specific binding domains. Specifically, lactate dehydrogenase and NADH oxidase were fused with a cellulose binding domain, which enabled both enzyme recovery and assembling in essentially one single step by using NFC. Results showed that the binding capacity of the enzymes was as high as 0.9 μmol-enzyme/g-NFC. Compared to native parent free enzymes, NFC-enzyme assemblies improved the catalytic efficiency of the coupled reaction system by over 100%. The lifetime of enzymes was also improved by as high as 27 folds. The work demonstrates promising potential of using biocompatible and environmentally benign bio-based nanomaterials for construction of efficient catalysts for intensified bioprocessing and biotransformation applications.

Original languageEnglish (US)
Pages (from-to)1369-1383
Number of pages15
JournalApplied Biochemistry and Biotechnology
Volume191
Issue number4
DOIs
StatePublished - Aug 1 2020

Bibliographical note

Funding Information:
Dai thanks Chinese Scholarship Council for the support of an international scholarship for visiting research at UMN. Branciforti is grateful to CAPES (project Nanobiotec number 13; postdoctoral scholarship for process number 6290-13-2) for funding her research at the University of Minnesota. Wang thanks partial support from IPRIME (Industrial Partnership for Research in Interfacial and Materials Engineering) of University of Minnesota.

Keywords

  • Cellulose binding domain
  • Cofactor regeneration
  • Lactate dehydrogenase
  • NADH oxidase
  • Nanocellulose

PubMed: MeSH publication types

  • Journal Article

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