Abstract
Although microbial transglutaminases (mTGs) were initially discovered to offset the cost of producing mammalian transglutaminases for food applications, they have quickly become important tools in research and biotechnology. Today, mTGs are utilized for a large number of applications to conjugate proteins and peptides to small molecules, polymers, surfaces, and DNA, as well as to other proteins. It is important to know how to maximize the advantages of the enzymatic approach and avoid undesired cross-linking. This review focuses on the versatility of transglutaminases in the field of bioconjugation and covers recent developments in utilizing mTG for generating antibody drug conjugates (ADCs) for therapeutic applications.
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