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Application of a rational crystal contact engineering strategy on a poly(ethylene terephthalate)-degrading cutinase.
Bioengineering 12, 561 - 561 (2025)
Publ. Version/Full Text
DOI
PMC
Industrial biotechnology offers a potential ecological solution for PET
recycling under relatively mild reaction conditions via enzymatic
degradation, particularly using the leaf branch compost cutinase (LCC)
quadruple mutant ICCG. To improve the efficient downstream processing of
this biocatalyst after heterologous gene expression with a suitable
production host, protein crystallization can serve as an effective
purification/capture step. Enhancing protein crystallization was
achieved in recent studies by introducing electrostatic (and aromatic)
interactions in two homologous alcohol dehydrogenases (Lb/LkADH) and an ene reductase (NspER1-L1,5) produced with Escherichia coli.
In this study, ICCG, which is difficult to crystallize, was utilized
for the application of crystal contact engineering strategies, resulting
in ICCG mutant L50Y (ICCGY). Previously focused on the Lys-Glu
interaction for the introduction of electrostatic interactions at
crystal contacts, the applicability of the engineering strategy was
extended here to an Arg-Glu interaction to increase crystallizability,
as shown for ICCGY T110E. Furthermore, the rationale of the engineering
approach is demonstrated by introducing Lys and Glu at non-crystal
contacts or sites without potential interaction partners as negative
controls. These resulting mutants crystallized comparably but not
superior to the wild-type protein. As demonstrated by this study,
crystal contact engineering emerges as a promising approach for
rationally enhancing protein crystallization. This advancement could
significantly streamline biotechnological downstream processing,
offering a more efficient pathway for research and industry.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
protein engineering; crystallization; PET-degrading cutinase; downstream processing
ISSN (print) / ISBN
2306-5354
Journal
Bioengineering
Quellenangaben
Volume: 12,
Issue: 6,
Pages: 561 - 561
Publisher
MDPI
Publishing Place
Basel
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Deutsche Forschungsgemeinschaft