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White to light yellow to dark brown powder or granules, or a clear light yellow to dark brown liquid. It is soluble in water, insoluble in ethanol, and hygroscopic. It can convert α-glutamyl groups in protein peptides into ε-amino groups of lysine residues in peptides. Transglutaminase catalyzes cross-linking reactions, modifying proteins and improving their plasticity, water retention, solubility, and functionality. As a protein modifier, it has great application prospects in the food industry. Currently, it is widely used in meat, dairy, and plant protein products to improve product quality. In noodle processing, the addition of transglutaminase can promote cross-linking between other proteins and gluten, improving the gluten network structure and thus enhancing the quality of the finished noodles.

Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptides. Liver transglutaminase is a nonzymogenic enzyme.