Biocatalysis by transglutaminases: a review of biotechnological applications

Savoca, M.P. ORCID: 0000-0002-6465-341X, Tonoli, E. ORCID: 0000-0001-9774-1048, Atobatele, A.G. ORCID: 0000-0002-9182-6742 and Verderio, E.A.M. ORCID: 0000-0001-9153-8997, 2018. Biocatalysis by transglutaminases: a review of biotechnological applications. Micromachines, 9 (11): 562. ISSN 2072-666X

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Abstract

The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications.

Item Type: Journal article
Publication Title: Micromachines
Creators: Savoca, M.P., Tonoli, E., Atobatele, A.G. and Verderio, E.A.M.
Publisher: MDPI
Date: 31 October 2018
Volume: 9
Number: 11
ISSN: 2072-666X
Identifiers:
NumberType
10.3390/mi9110562DOI
mi9110562Publisher Item Identifier
Rights: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
Divisions: Schools > School of Science and Technology
Depositing User: Jonathan Gallacher
Date Added: 29 Nov 2018 14:22
Last Modified: 29 Nov 2018 14:22
URI: http://irep.ntu.ac.uk/id/eprint/35174

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