ArticleFrontiers in bioengineering and biotechnology2020
Multi-Enzyme Assembly on T4 Phage Scaffold.
Article in Frontiers in bioengineering and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 21 citations in OpenAlex.
- Biological Nanoscaffolds from Hierarchical Construction to Applications.Molecules (Basel, Switzerland) · 2026Review
- Isolation, characterization and whole genome analysis of the novel genus Lederbergvirus, phage vB_EcoP_E212 infecting enterotoxigenic Escherichia coli K88.Virus research · 2023Article
- Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Over the past two decades, various scaffolds have been designed and synthesized to organize enzyme cascades spatially for enhanced enzyme activity based on the concepts of substrate channeling and enhanced stability. The most bio-compatible synthetic scaffolds known for enzyme immobilization are protein and DNA nanostructures. Herein, we examined the utility of the T4 phage capsid to serve as a naturally occurring protein scaffold for the immobilization of a three-enzyme cascade: Amylase, Maltase, and Glucokinase. Covalent constructs between each of the enzymes and the outer capsid protein Hoc were prepared through SpyTag-SpyCatcher pairing and assembled onto phage capsids
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