Microbial Transglutaminase
Cat. Number: FA-00362
Size: 5g, 10g, 25g, Custom size
Description
Transglutaminase catalyzes cross-linking reactions to modify proteins and improve their plasticity, water holding capacity, water solubility and functionality.
Product Details
CAS Number
80146-85-6
Enzyme Commission Number
2.3.2.13
Synonyms
Protein-Glutamine-γ-Glutamyltransferase, Protein-glutamine:amine γ-glutamyltransferase
Source
Guinea pig liver
Application
Glutamine transaminase, abbreviated as TG, is an acyltransferase, an enzyme that catalyzes the inter-protein (or intra) acyl transfer reaction, resulting in covalent cross-linking between proteins (or polypeptides), thereby improving protein structure and Functional properties, giving food proteins a unique texture and taste. Therefore, transglutaminase has been widely used in food processing industries such as meat products, aquatic products and dairy products.
Appearance
Lyophilized powder
Activity
≥12 units/mg
Molecular Weight
76.6 kDa
Storage Temp.
-20 °C
Handling Precaution
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.
Handling Precaution
One unit will catalyze the formation of 1.0 μmole of hydroxamate per min from Nα-Z-Gln-Gly and hydroxylamine at pH 6.0 at 37 °C. (L-Glutamic acid γ-monohydroxamate is the standard.)
For Research Use Only!
