دورية أكاديمية

Data-driven enzyme immobilisation: a case study using DNA to immobilise galactose oxidase

التفاصيل البيبلوغرافية
العنوان: Data-driven enzyme immobilisation: a case study using DNA to immobilise galactose oxidase
المؤلفون: Wolfgang Ott, Alessandro Ceccarelli, Jack Manning, Nicholas J. Turner, Robert Oppenheimer
المصدر: Engineering Biology (2020)
بيانات النشر: Wiley, 2020.
سنة النشر: 2020
المجموعة: LCC:Biology (General)
مصطلحات موضوعية: molecular biophysics, catalysis, enzymes, dna, biochemistry, green chemistry, enzyme stability, product purification, reaction conditions, deoxyribonucleic acid, supramolecular scaffolds, simple watson–crick base-pairing rules, unique nanoscale environment, individual enzyme, enzyme activity, dna nanostructures, relevant chemical syntheses, galactose oxidase mutant, crude biocatalytic reactions, data-driven enzyme immobilisation, deoxyribonucleic acid stands, Biology (General), QH301-705.5
الوصف: Biocatalysis has the potential to enable green chemistry. New methods of enzyme immobilisation will be required to improve enzyme stability, product purification, and compatibility of different enzymes in the same reaction conditions. Deoxyribonucleic acid (DNA) stands out among supramolecular scaffolds, as simple Watson–Crick base-pairing rules can be used to rationally design a unique nanoscale environment around each individual enzyme in a cascade. Enhancements of enzyme activity and stability on DNA nanostructures have previously been reported, but never in the context of industrially relevant chemical syntheses or reaction conditions. Here, the authors show DNA can enhance the activity and stability of a galactose oxidase mutant, which could be used in a cascade to produce bioplastics from lignin. The enzyme was enhanced in the cell-free extract, which to their knowledge has not been shown before for any enzymes on DNA. This is significant because crude biocatalytic reactions are vastly more cost-effective. This opens the door to further work on multienzyme cascades by tuning the properties of individual enzymes.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2398-6182
Relation: https://digital-library.theiet.org/content/journals/10.1049/enb.2020.0014; https://doaj.org/toc/2398-6182
DOI: 10.1049/enb.2020.0014
URL الوصول: https://doaj.org/article/90f545fcbf964693844c3a146a55c2a6
رقم الأكسشن: edsdoj.90f545fcbf964693844c3a146a55c2a6
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:23986182
DOI:10.1049/enb.2020.0014